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44 results on '"Engilberge S"'

1. CryoRhodopsins: a comprehensive characterization of a new clade of microbial rhodopsins from cold environments

Author

Lamm, G.H.U., primary, Marin, E., additional, Schellbach, A.V., additional, Stetsenko, A., additional, Alekseev, A., additional, Bourenkov, G., additional, Borshchevskiy, V., additional, Asido, M., additional, Agthe, M., additional, Engilberge, S., additional, Rose, S.L., additional, Caramello, N., additional, Royant, A., additional, Schneider, T. R., additional, Bateman, A., additional, Mager, T., additional, Moser, T., additional, Wachtveitl, J., additional, Guskov, A., additional, and Kovalev, K., additional

Published
2024
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2. TR-SFX MmCPDII-DNA complex: 500 ns time-point collected in SACLA. Includes 500 ns, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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3. TR-SFX MmCPDII-DNA complex: 250 ps snapshot. Includes 250 ps, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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4. TR-SFX MmCPDII-DNA complex: 2 ns snapshot. Includes 2 ns, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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5. TR-SFX MmCPDII-DNA complex: 100 ps snapshot. Includes 100ps, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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6. TR-SFX MmCPDII-DNA complex: 10 ns time-point collected in SACLA. Includes 10 ns, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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7. TR-SFX MmCPDII-DNA complex: 25 us time-point collected in SACLA. Includes 25 us, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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8. TR-SFX MmCPDII-DNA complex: 3.35 ns snapshot. Includes 3.35 ns, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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9. TR-SFX MmCPDII-DNA complex: dark state as collected in SACLA

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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10. Dark, fully reduced structure of the MmCPDII-DNA complex as produced at SwissFEL

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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11. DF-SFX MmCPDII-DNA complex: steady state oxidized complex

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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12. TR-SFX MmCPDII-DNA complex: 6 ns snapshot. Includes 6 ns, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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13. TR-SFX MmCPDII-DNA complex: 650 ps snapshot. Includes 650ps, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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14. TR-SFX MmCPDII-DNA complex: 450 ps snapshot. Includes 450ps, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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15. TR-SFX MmCPDII-DNA complex: 10 ns snapshot. Includes 10 ns, dark, and extrapolated structure factors. Collected at SwissFEL

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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16. TR-SFX MmCPDII-DNA complex: 1 ns snapshot. Includes 1 ns, dark, and extrapolated structure factors

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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17. MmCPDII-DNA complex containing low-dosage, light induced repaired DNA.

Author

Maestre-Reyna, M., primary, Wang, P.-H., additional, Nango, E., additional, Hosokawa, Y., additional, Saft, M., additional, Furrer, A., additional, Yang, C.-H., additional, Ngura Putu, E.P.G., additional, Wu, W.-J., additional, Emmerich, H.-J., additional, Engilberge, S., additional, Caramello, N., additional, Wranik, M., additional, Glover, H.L., additional, Franz-Badur, S., additional, Wu, H.-Y., additional, Lee, C.-C., additional, Huang, W.-C., additional, Huang, K.-F., additional, Chang, Y.-K., additional, Liao, J.-H., additional, Weng, J.-H., additional, Gad, W., additional, Chang, C.-W., additional, Pang, A.H., additional, Gashi, D., additional, Beale, E., additional, Ozerov, D., additional, Milne, C., additional, Cirelli, C., additional, Bacellar, C., additional, Sugahara, M., additional, Owada, S., additional, Joti, Y., additional, Yamashita, A., additional, Tanaka, R., additional, Tanaka, T., additional, Luo, F.J., additional, Tono, K., additional, Kiontke, S., additional, Spadaccini, R., additional, Royant, A., additional, Yamamoto, J., additional, Iwata, S., additional, Standfuss, J., additional, Essen, L.-O., additional, Bessho, Y., additional, and Tsai, M.-D., additional

Published
2023
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20. Chimpanzee CPEB3 HDV-like ribozyme

Author

Przytula-Mally, A.I., primary, Engilberge, S., additional, Johannsen, S., additional, Olieric, V., additional, Masquida, B., additional, and Sigel, R.K.O., additional

Published
2022
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21. human CPEB3 HDV-like ribozyme

Author

Przytula-Mally, A.I., primary, Engilberge, S., additional, Johannsen, S., additional, Olieric, V., additional, Masquida, B., additional, and Sigel, R.K.O., additional

Published
2022
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32. Protein crystallization and structure determination at room temperature in the CrystalChip.

Author

Pachl P, Coudray L, Vincent R, Nilles L, Scheer H, Ritzenthaler C, Fejfarová A, Řezáčová P, Engilberge S, and Sauter C

Abstract

The production of high-quality crystals is a key step in crystallography in general, but control of crystallization conditions is even more crucial in serial crystallography, which requires sets of crystals homogeneous in size and diffraction properties. This protocol describes the implementation of a simple and user-friendly microfluidic device that allows both the production of crystals by the counter-diffusion method and their in situ analysis by serial crystallography. As an illustration, the whole procedure is used to determine the crystal structure of three proteins from data collected at room temperature at a synchrotron radiation source., (© 2024 The Author(s). FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)

Published
2024
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33. Does Acinetobacter calcoaceticus glucose dehydrogenase produce self-damaging H2O2?

Author

Lublin V, Kauffmann B, Engilberge S, Durola F, Gounel S, Bichon S, Jean C, Mano N, Giraud MF, Chavas LMGH, Thureau A, Thompson A, and Stines-Chaumeil C

Subjects
Crystallography, X-Ray, Glucose metabolism, Mutation, PQQ Cofactor metabolism, Substrate Specificity, Acinetobacter calcoaceticus enzymology, Acinetobacter calcoaceticus genetics, Bacterial Proteins genetics, Bacterial Proteins metabolism, Glucose 1-Dehydrogenase genetics, Glucose 1-Dehydrogenase metabolism, Hydrogen Peroxide metabolism
Abstract

The soluble glucose dehydrogenase (sGDH) from Acinetobacter calcoaceticus has been widely studied and is used, in biosensors, to detect the presence of glucose, taking advantage of its high turnover and insensitivity to molecular oxygen. This approach, however, presents two drawbacks: the enzyme has broad substrate specificity (leading to imprecise blood glucose measurements) and shows instability over time (inferior to other oxidizing glucose enzymes). We report the characterization of two sGDH mutants: the single mutant Y343F and the double mutant D143E/Y343F. The mutants present enzyme selectivity and specificity of 1.2 (Y343F) and 5.7 (D143E/Y343F) times higher for glucose compared with that of the wild-type. Crystallographic experiments, designed to characterize these mutants, surprisingly revealed that the prosthetic group PQQ (pyrroloquinoline quinone), essential for the enzymatic activity, is in a cleaved form for both wild-type and mutant structures. We provide evidence suggesting that the sGDH produces H2O2, the level of production depending on the mutation. In addition, spectroscopic experiments allowed us to follow the self-degradation of the prosthetic group and the disappearance of sGDH's glucose oxidation activity. These studies suggest that the enzyme is sensitive to its self-production of H2O2. We show that the premature aging of sGDH can be slowed down by adding catalase to consume the H2O2 produced, allowing the design of a more stable biosensor over time. Our research opens questions about the mechanism of H2O2 production and the physiological role of this activity by sGDH., (© 2024 The Author(s).)

Published
2024
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34. A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron-binding protein FutA from Prochlorococcus .

Author

Bolton R, Machelett MM, Stubbs J, Axford D, Caramello N, Catapano L, Malý M, Rodrigues MJ, Cordery C, Tizzard GJ, MacMillan F, Engilberge S, von Stetten D, Tosha T, Sugimoto H, Worrall JAR, Webb JS, Zubkov M, Coles S, Mathieu E, Steiner RA, Murshudov G, Schrader TE, Orville AM, Royant A, Evans G, Hough MA, Owen RL, and Tews I

Subjects
Iron-Binding Proteins metabolism, Iron metabolism, Oxidation-Reduction, Transferrin metabolism, Water chemistry, Ferrous Compounds chemistry, Crystallography, X-Ray, Ferric Compounds chemistry, Prochlorococcus metabolism
Abstract

The marine cyanobacterium Prochlorococcus is a main contributor to global photosynthesis, whilst being limited by iron availability. Cyanobacterial genomes generally encode two different types of FutA iron-binding proteins: periplasmic FutA2 ABC transporter subunits bind Fe(III), while cytosolic FutA1 binds Fe(II). Owing to their small size and their economized genome Prochlorococcus ecotypes typically possess a single futA gene. How the encoded FutA protein might bind different Fe oxidation states was previously unknown. Here, we use structural biology techniques at room temperature to probe the dynamic behavior of FutA. Neutron diffraction confirmed four negatively charged tyrosinates, that together with a neutral water molecule coordinate iron in trigonal bipyramidal geometry. Positioning of the positively charged Arg103 side chain in the second coordination shell yields an overall charge-neutral Fe(III) binding state in structures determined by neutron diffraction and serial femtosecond crystallography. Conventional rotation X-ray crystallography using a home source revealed X-ray-induced photoreduction of the iron center with observation of the Fe(II) binding state; here, an additional positioning of the Arg203 side chain in the second coordination shell maintained an overall charge neutral Fe(II) binding site. Dose series using serial synchrotron crystallography and an XFEL X-ray pump-probe approach capture the transition between Fe(III) and Fe(II) states, revealing how Arg203 operates as a switch to accommodate the different iron oxidation states. This switching ability of the Prochlorococcus FutA protein may reflect ecological adaptation by genome streamlining and loss of specialized FutA proteins., Competing Interests: Competing interests statement:The authors declare no competing interest.

Published
2024
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35. Peptide-Based Covalent Inhibitors Bearing Mild Electrophiles to Target a Conserved His Residue of the Bacterial Sliding Clamp.

Author

Compain G, Monsarrat C, Blagojevic J, Brillet K, Dumas P, Hammann P, Kuhn L, Martiel I, Engilberge S, Oliéric V, Wolff P, Burnouf DY, Wagner J, and Guichard G

Abstract

Peptide-based covalent inhibitors targeted to nucleophilic protein residues have recently emerged as new modalities to target protein-protein interactions (PPIs) as they may provide some benefits over more classic competitive inhibitors. Covalent inhibitors are generally targeted to cysteine, the most intrinsically reactive amino acid residue, and to lysine, which is more abundant at the surface of proteins but much less frequently to histidine. Herein, we report the structure-guided design of targeted covalent inhibitors (TCIs) able to bind covalently and selectively to the bacterial sliding clamp (SC), by reacting with a well-conserved histidine residue located on the edge of the peptide-binding pocket. SC is an essential component of the bacterial DNA replication machinery, identified as a promising target for the development of new antibacterial compounds. Thermodynamic and kinetic analyses of ligands bearing different mild electrophilic warheads confirmed the higher efficiency of the chloroacetamide compared to Michael acceptors. Two high-resolution X-ray structures of covalent inhibitor-SC adducts were obtained, revealing the canonical orientation of the ligand and details of covalent bond formation with histidine. Proteomic studies were consistent with a selective SC engagement by the chloroacetamide-based TCI. Finally, the TCI of SC was substantially more active than the parent noncovalent inhibitor in an in vitro SC-dependent DNA synthesis assay, validating the potential of the approach to design covalent inhibitors of protein-protein interactions targeted to histidine., Competing Interests: The authors declare no competing financial interest., (© 2024 The Authors. Published by American Chemical Society.)

Published
2024
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36. The TR-icOS setup at the ESRF: time-resolved microsecond UV-Vis absorption spectroscopy on protein crystals.

Author

Engilberge S, Caramello N, Bukhdruker S, Byrdin M, Giraud T, Jacquet P, Scortani D, Biv R, Gonzalez H, Broquet A, van der Linden P, Rose SL, Flot D, Balandin T, Gordeliy V, Lahey-Rudolph JM, Roessle M, de Sanctis D, Leonard GA, Mueller-Dieckmann C, and Royant A

Subjects
Spectrum Analysis, Crystallography, Light, Proteins chemistry, Synchrotrons
Abstract

The technique of time-resolved macromolecular crystallography (TR-MX) has recently been rejuvenated at synchrotrons, resulting in the design of dedicated beamlines. Using pump-probe schemes, this should make the mechanistic study of photoactive proteins and other suitable systems possible with time resolutions down to microseconds. In order to identify relevant time delays, time-resolved spectroscopic experiments directly performed on protein crystals are often desirable. To this end, an instrument has been built at the icOS Lab (in crystallo Optical Spectroscopy Laboratory) at the European Synchrotron Radiation Facility using reflective focusing objectives with a tuneable nanosecond laser as a pump and a microsecond xenon flash lamp as a probe, called the TR-icOS (time-resolved icOS) setup. Using this instrument, pump-probe spectra can rapidly be recorded from single crystals with time delays ranging from a few microseconds to seconds and beyond. This can be repeated at various laser pulse energies to track the potential presence of artefacts arising from two-photon absorption, which amounts to a power titration of a photoreaction. This approach has been applied to monitor the rise and decay of the M state in the photocycle of crystallized bacteriorhodopsin and showed that the photocycle is increasingly altered with laser pulses of peak fluence greater than 100 mJ cm -2 , providing experimental laser and delay parameters for a successful TR-MX experiment., (open access.)

Published
2024
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37. Visualizing the DNA repair process by a photolyase at atomic resolution.

Author

Maestre-Reyna M, Wang PH, Nango E, Hosokawa Y, Saft M, Furrer A, Yang CH, Gusti Ngurah Putu EP, Wu WJ, Emmerich HJ, Caramello N, Franz-Badur S, Yang C, Engilberge S, Wranik M, Glover HL, Weinert T, Wu HY, Lee CC, Huang WC, Huang KF, Chang YK, Liao JH, Weng JH, Gad W, Chang CW, Pang AH, Yang KC, Lin WT, Chang YC, Gashi D, Beale E, Ozerov D, Nass K, Knopp G, Johnson PJM, Cirelli C, Milne C, Bacellar C, Sugahara M, Owada S, Joti Y, Yamashita A, Tanaka R, Tanaka T, Luo F, Tono K, Zarzycka W, Müller P, Alahmad MA, Bezold F, Fuchs V, Gnau P, Kiontke S, Korf L, Reithofer V, Rosner CJ, Seiler EM, Watad M, Werel L, Spadaccini R, Yamamoto J, Iwata S, Zhong D, Standfuss J, Royant A, Bessho Y, Essen LO, and Tsai MD

Subjects
Catalysis, Crystallography methods, DNA chemistry, DNA radiation effects, Protein Conformation, Ultraviolet Rays, Archaeal Proteins chemistry, Deoxyribodipyrimidine Photo-Lyase chemistry, DNA Repair, Methanosarcina enzymology, Pyrimidine Dimers chemistry
Abstract

Photolyases, a ubiquitous class of flavoproteins, use blue light to repair DNA photolesions. In this work, we determined the structural mechanism of the photolyase-catalyzed repair of a cyclobutane pyrimidine dimer (CPD) lesion using time-resolved serial femtosecond crystallography (TR-SFX). We obtained 18 snapshots that show time-dependent changes in four reaction loci. We used these results to create a movie that depicts the repair of CPD lesions in the picosecond-to-nanosecond range, followed by the recovery of the enzymatic moieties involved in catalysis, completing the formation of the fully reduced enzyme-product complex at 500 nanoseconds. Finally, back-flip intermediates of the thymine bases to reanneal the DNA were captured at 25 to 200 microseconds. Our data cover the complete molecular mechanism of a photolyase and, importantly, its chemistry and enzymatic catalysis at work across a wide timescale and at atomic resolution.

Published
2023
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38. Molecular characterization of accripin11, a soluble shell protein with an acidic C-terminus, identified in the prismatic layer of the Mediterranean fan mussel Pinna nobilis (Bivalvia, Pteriomorphia).

Author

Khurshid B, Jackson DJ, Engilberge S, Motreuil S, Broussard C, Thomas J, Immel F, Harrington MJ, Crowley PB, Vielzeuf D, Perrin J, and Marin F

Subjects
Animals, Proteins chemistry, Calcium Carbonate metabolism, Aspartic Acid, Proteomics, Bivalvia genetics, Bivalvia chemistry, Bivalvia metabolism
Abstract

We have identified a novel shell protein, accripin11, as a major soluble component of the calcitic prisms of the fan mussel Pinna nobilis. Initially retrieved from a cDNA library, its full sequence is confirmed here by transcriptomic and proteomic approaches. The sequence of the mature protein is 103 residues with a theoretical molecular weight of 11 kDa and is moderately acidic (pI 6.74) except for its C-terminus which is highly enriched in aspartic acid. The protein exhibits a peculiar cysteine pattern in its central domain. The full sequence shares similarity with six other uncharacterized molluscan shell proteins from the orders Ostreida, Pteriida and Mytilida, all of which are pteriomorphids and produce a phylogenetically restricted pattern of nacro-prismatic shell microstructures. This suggests that accripin11 is a member of a family of clade-specific shell proteins. A 3D model of accripin11 was predicted with AlphaFold2, indicating that it possesses three short alpha helices and a disordered C-terminus. Recombinant accripin11 was tested in vitro for its ability to influence the crystallization of CaCO 3 , while a polyclonal antibody was able to locate accripin11 to prismatic extracts, particularly in the acetic acid-soluble matrix. The putative functions of accripin11 are further discussed in relation to shell biomineralization., (© 2022 The Authors. FEBS Open Bio published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.)

Published
2023
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39. Filling of a water-free void explains the allosteric regulation of the β 1 -adrenergic receptor by cholesterol.

Author

Abiko LA, Dias Teixeira R, Engilberge S, Grahl A, Mühlethaler T, Sharpe T, and Grzesiek S

Subjects
Allosteric Regulation, Cholesterol, Isoproterenol, Xenon, Detergents, Receptors, G-Protein-Coupled
Abstract

Recent high-pressure NMR results indicate that the preactive conformation of the β 1 -adrenergic receptor (β 1 AR) harbours completely empty cavities of ~100 Å 3 volume, which disappear in the active conformation of the receptor. Here we have localized these cavities using X-ray crystallography of xenon-derivatized β 1 AR crystals. One of the cavities is in direct contact with the cholesterol-binding pocket. Solution NMR shows that addition of the cholesterol analogue cholesteryl hemisuccinate impedes the formation of the active conformation of detergent-solubilized β 1 AR by blocking conserved G protein-coupled receptor microswitches, concomitant with an affinity reduction of both isoprenaline and G protein-mimicking nanobody Nb80 for β 1 AR detected by isothermal titration calorimetry. This wedge-like action explains the function of cholesterol as a negative allosteric modulator of β 1 AR. A detailed understanding of G protein-coupled receptor regulation by cholesterol by filling of a dry void and the easy scouting for such voids by xenon may provide new routes for the development of allosteric drugs., (© 2022. The Author(s), under exclusive licence to Springer Nature Limited.)

Published
2022
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40. Slow protein dynamics probed by time-resolved oscillation crystallography at room temperature.

Author

Aumonier S, Engilberge S, Caramello N, von Stetten D, Gotthard G, Leonard GA, Mueller-Dieckmann C, and Royant A

Abstract

The development of serial crystallography over the last decade at XFELs and synchrotrons has produced a renaissance in room-temperature macromolecular crystallography (RT-MX), and fostered many technical and methodological breakthroughs designed to study phenomena occurring in proteins on the picosecond-to-second timescale. However, there are components of protein dynamics that occur in much slower regimes, of which the study could readily benefit from state-of-the-art RT-MX. Here, the room-temperature structural study of the relaxation of a reaction intermediate at a synchrotron, exploiting a handful of single crystals, is described. The intermediate in question is formed in microseconds during the photoreaction of the LOV2 domain of phototropin 2 from Arabidopsis thaliana , which then decays in minutes. This work monitored its relaxation in the dark using a fast-readout EIGER X 4M detector to record several complete oscillation X-ray diffraction datasets, each of 1.2 s total exposure time, at different time points in the relaxation process. Coupled with in crystallo UV-Vis absorption spectroscopy, this RT-MX approach allowed the authors to follow the relaxation of the photoadduct, a thio-ether covalent bond between the chromophore and a cysteine residue. Unexpectedly, the return of the chromophore to its spectroscopic ground state is followed by medium-scale protein rearrangements that trigger a crystal phase transition and hinder the full recovery of the structural ground state of the protein. In addition to suggesting a hitherto unexpected role of a conserved tryptophan residue in the regulation of the photocycle of LOV2, this work provides a basis for performing routine time-resolved protein crystallography experiments at synchrotrons for phenomena occurring on the second-to-hour timescale., (© Sylvain Aumonier et al. 2022.)

Published
2022
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41. Medical contrast agents as promising tools for biomacromolecular SAXS experiments.

Author

Gabel F, Engilberge S, Schmitt E, Thureau A, Mechulam Y, Pérez J, and Girard E

Subjects
Iohexol, Proteins chemistry, RNA chemistry, Scattering, Small Angle, Solvents, X-Ray Diffraction, Contrast Media, Lanthanoid Series Elements
Abstract

Small-angle X-ray scattering (SAXS) has become an indispensable tool in structural biology, complementing atomic-resolution techniques. It is sensitive to the electron-density difference between solubilized biomacromolecules and the buffer, and provides information on molecular masses, particle dimensions and interactions, low-resolution conformations and pair distance-distribution functions. When SAXS data are recorded at multiple contrasts, i.e. at different solvent electron densities, it is possible to probe, in addition to their overall shape, the internal electron-density profile of biomacromolecular assemblies. Unfortunately, contrast-variation SAXS has been limited by the range of solvent electron densities attainable using conventional co-solutes (for example sugars, glycerol and salt) and by the fact that some biological systems are destabilized in their presence. Here, SAXS contrast data from an oligomeric protein and a protein-RNA complex are presented in the presence of iohexol and Gd-HPDO3A, two electron-rich molecules that are used in biomedical imaging and that belong to the families of iodinated and lanthanide-based complexes, respectively. Moderate concentrations of both molecules allowed solvent electron densities matching those of proteins to be attained. While iohexol yielded higher solvent electron densities (per mole), it interacted specifically with the oligomeric protein and precipitated the protein-RNA complex. Gd-HPDO3A, while less efficient (per mole), did not disrupt the structural integrity of either system, and atomic models could be compared with the SAXS data. Due to their elevated solubility and electron density, their chemical inertness, as well as the possibility of altering their physico-chemical properties, lanthanide-based complexes represent a class of molecules with promising potential for contrast-variation SAXS experiments on diverse biomacromolecular systems., (open access.)

Published
2022
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42. Probing ligand binding of endothiapepsin by `temperature-resolved' macromolecular crystallography.

Author

Huang CY, Aumonier S, Engilberge S, Eris D, Smith KML, Leonarski F, Wojdyla JA, Beale JH, Buntschu D, Pauluhn A, Sharpe ME, Metz A, Olieric V, and Wang M

Subjects
Aspartic Acid Endopeptidases, Crystallography, X-Ray, Ligands, Macromolecular Substances, Temperature, Proteins chemistry
Abstract

Continuous developments in cryogenic X-ray crystallography have provided most of our knowledge of 3D protein structures, which has recently been further augmented by revolutionary advances in cryoEM. However, a single structural conformation identified at cryogenic temperatures may introduce a fictitious structure as a result of cryogenic cooling artefacts, limiting the overview of inherent protein physiological dynamics, which play a critical role in the biological functions of proteins. Here, a room-temperature X-ray crystallographic method using temperature as a trigger to record movie-like structural snapshots has been developed. The method has been used to show how TL00150, a 175.15 Da fragment, undergoes binding-mode changes in endothiapepsin. A surprising fragment-binding discrepancy was observed between the cryo-cooled and physiological temperature structures, and multiple binding poses and their interplay with DMSO were captured. The observations here open up new promising prospects for structure determination and interpretation at physiological temperatures with implications for structure-based drug discovery., (open access.)

Published
2022
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43. De novo determination of mosquitocidal Cry11Aa and Cry11Ba structures from naturally-occurring nanocrystals.

Author

Tetreau G, Sawaya MR, De Zitter E, Andreeva EA, Banneville AS, Schibrowsky NA, Coquelle N, Brewster AS, Grünbein ML, Kovacs GN, Hunter MS, Kloos M, Sierra RG, Schiro G, Qiao P, Stricker M, Bideshi D, Young ID, Zala N, Engilberge S, Gorel A, Signor L, Teulon JM, Hilpert M, Foucar L, Bielecki J, Bean R, de Wijn R, Sato T, Kirkwood H, Letrun R, Batyuk A, Snigireva I, Fenel D, Schubert R, Canfield EJ, Alba MM, Laporte F, Després L, Bacia M, Roux A, Chapelle C, Riobé F, Maury O, Ling WL, Boutet S, Mancuso A, Gutsche I, Girard E, Barends TRM, Pellequer JL, Park HW, Laganowsky AD, Rodriguez J, Burghammer M, Shoeman RL, Doak RB, Weik M, Sauter NK, Federici B, Cascio D, Schlichting I, and Colletier JP

Subjects
Animals, Bacterial Proteins toxicity, Endotoxins, Hemolysin Proteins toxicity, Larva, Mosquito Control, Bacillus thuringiensis, Nanoparticles
Abstract

Cry11Aa and Cry11Ba are the two most potent toxins produced by mosquitocidal Bacillus thuringiensis subsp. israelensis and jegathesan, respectively. The toxins naturally crystallize within the host; however, the crystals are too small for structure determination at synchrotron sources. Therefore, we applied serial femtosecond crystallography at X-ray free electron lasers to in vivo-grown nanocrystals of these toxins. The structure of Cry11Aa was determined de novo using the single-wavelength anomalous dispersion method, which in turn enabled the determination of the Cry11Ba structure by molecular replacement. The two structures reveal a new pattern for in vivo crystallization of Cry toxins, whereby each of their three domains packs with a symmetrically identical domain, and a cleavable crystal packing motif is located within the protoxin rather than at the termini. The diversity of in vivo crystallization patterns suggests explanations for their varied levels of toxicity and rational approaches to improve these toxins for mosquito control., (© 2022. The Author(s).)

Published
2022
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44. Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology.

Author

Collu G, Bierig T, Krebs AS, Engilberge S, Varma N, Guixà-González R, Sharpe T, Deupi X, Olieric V, Poghosyan E, and Benoit RM

Subjects
Cryoelectron Microscopy, Crystallography, X-Ray, Models, Molecular, Molecular Dynamics Simulation, Nanoparticles, Protein Structure, Secondary, Epitopes chemistry, Recombinant Fusion Proteins chemistry
Abstract

Chimeric fusion proteins are essential tools for protein nanotechnology. Non-optimized protein-protein connections are usually flexible and therefore unsuitable as structural building blocks. Here we show that the ER/K motif, a single α-helical domain (SAH), can be seamlessly fused to terminal helices of proteins, forming an extended, partially free-standing rigid helix. This enables the connection of two domains at a defined distance and orientation. We designed three constructs termed YFPnano, T4Lnano, and MoStoNano. Analysis of experimentally determined structures and molecular dynamics simulations reveals a certain degree of plasticity in the connections that allows the adaptation to crystal contact opportunities. Our data show that SAHs can be stably integrated into designed structural elements, enabling new possibilities for protein nanotechnology, for example, to improve the exposure of epitopes on nanoparticles (structural vaccinology), to engineer crystal contacts with minimal impact on construct flexibility (for the study of protein dynamics), and to design novel biomaterials., Competing Interests: Declaration of interests The authors declare no competing interests., (Copyright © 2021. Published by Elsevier Ltd.)

Published
2022
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