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Start Over Descriptor "solutionless crystal mount" Topic eisenia
2 results on '"solutionless crystal mount"'

1. Crystallographic analysis of Eisenia hydrolysis‐enhancing protein using a long wavelength for native‐SAD phasing.

Author

Sun, Xiaomei, Ye, Yuxin, Sakurai, Naofumi, Kato, Koji, Yuasa, Keizo, Tsuji, Akihiko, and Yao, Min

Subjects
*EISENIA, *BROWN algae, *WAVELENGTHS, *PROTEINS, *SPACE groups
Abstract

Eisenia hydrolysis‐enhancing protein (EHEP), which is a novel protein that has been identified in Aplysia kurodai, protects β‐glucosidases from phlorotannin inhibition to facilitate the production of glucose from the laminarin abundant in brown algae. Hence, EHEP has attracted attention for its potential applications in producing biofuel from brown algae. In this study, EHEP was purified from the natural digestive fluid of A. kurodai and was crystallized using the sitting‐drop vapor‐diffusion method. Native and SAD (single‐wavelength anomalous diffraction) data sets were successfully collected at resolutions of 1.20 and 2.48 Å using wavelengths of 1.0 and 2.1 Å, respectively, from crystals obtained in initial screening. The crystals belonged to space group P212121 and contained one EHEP molecule in the asymmetric unit. All 20 S‐atom sites in EHEP were located and the phases were determined by the SAD method using the S atoms in the natural protein as anomalous scatterers (native‐SAD). After phase improvement, interpretable electron densities were obtained and 58% of the model was automatically built. [ABSTRACT FROM AUTHOR]

Published
2020
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2. Crystallographic analysis of Eisenia hydrolysis-enhancing protein using a long wavelength for native-SAD phasing

Author

Xiaomei Sun, Koji Kato, Naofumi Sakurai, Yuxin Ye, Keizo Yuasa, Min Yao, and Akihiko Tsuji

Subjects
Models, Molecular, Protein Conformation, 020209 energy, Biophysics, solutionless crystal mount, 02 engineering and technology, Crystallography, X-Ray, Biochemistry, Phlorotannin, Mass Spectrometry, Research Communications, 03 medical and health sciences, Hydrolysis, Laminarin, chemistry.chemical_compound, Protein Domains, Structural Biology, Phase (matter), Aplysia, 0202 electrical engineering, electronic engineering, information engineering, Genetics, Molecule, Animals, phlorotannin binding, 030304 developmental biology, chemistry.chemical_classification, 0303 health sciences, biology, Chemistry, EHEP, native-SAD, Proteins, Condensed Matter Physics, biology.organism_classification, Phaser, Brown algae, Crystallography, Eisenia, biofuel, Crystallization
Abstract

Eisenia hydrolysis-enhancing protein (EHEP), which is a novel protein that has been identified in Aplysia kurodai, protects β-glucosidases from phlorotannin inhibition to facilitate the production of glucose from the laminarin abundant in brown algae. Hence, EHEP has attracted attention for its potential applications in producing biofuel from brown algae. In this study, EHEP was purified from the natural digestive fluid of A. kurodai and was crystallized using the sitting-drop vapor-diffusion method. Native and SAD (single-wavelength anomalous diffraction) data sets were successfully collected at resolutions of 1.20 and 2.48 Å using wavelengths of 1.0 and 2.1 Å, respectively, from crystals obtained in initial screening. The crystals belonged to space group P212121 and contained one EHEP molecule in the asymmetric unit. All 20 S-atom sites in EHEP were located and the phases were determined by the SAD method using the S atoms in the natural protein as anomalous scatterers (native-SAD). After phase improvement, interpretable electron densities were obtained and 58% of the model was automatically built.

Published
2020

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