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Your search keyword '"Liu, Shu-Hu"' showing total 14 results
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14 results on '"Liu, Shu-Hu"'

2. Devices for high precision x-ray beam intensity monitoring on BSRF

Author

Hua-Peng, LI, Tang, Kun, Zhao, Yi-Dong, Zheng, Lei, Liu, Shu-Hu, Zhao, Xiao-Liang, and Zhao, Ya-Shuai

Subjects
Physics - Instrumentation and Detectors, Nuclear Experiment
Abstract

Synchrotron radiation with the characteristic of high brilliance, high level of polarization, high collimation, low emittance and wide tunability in energy has been used as a standard source in metrology(1, 2). For a decade, lots of calibration work have been done on 4B7A in Beijing Synchrotron Radiation Facility (BSRF) (3, 4). For the calibration process, a high-precision online monitor is indispensable. To control the uncertainty under 0.1%, we studied different sizes parallel ion chambers with rare-gas and used different collecting methods to monitor the x-ray intensity of the beamline. Two methods to collect the signal of the ion chambers: reading the current directly with electrometer or signal amplification to collect the counts were compared., Comment: 7 pages

Published
2015

3. Vacuum ultraviolet photon detector with continuously adjustable resolution for inverse photoemission spectroscopy

Author

Liu, Shu-Hu, Hong, Cai-Hao, Zhao, Yi-Dong, Geng, Dong-Ping, Zheng, Lei, Zhao, Xiao-Liang, and Li, Hua-Peng

Subjects
Physics - Instrumentation and Detectors
Abstract

We present a vacuum ultraviolet (VUV) band-pass photon detector for inverse photoemission spectroscopy. A SrF2 window is used due to its high-energy cutoff of the optical transmission being 9.7eV, and acetone is selected as filling gas with the photoionization threshold also being 9.7eV. The structure of the detector described in detail is based on a Geiger-M\"uller type counter with an MgF2 window and argon as amplification gas. Its energy resolution can be tuned continuously from 46meV with a normal temperature situation to 105meV at 215K. Meanwhile, the signal intensity of the detector is adjusted accordingly to find an optimal operation program for our inverse photoemission system which is being constructed. The ratio of acetone vapor and argon is varied carefully. Background signals and the response of time are analyzed. The detector is normalized by deuterium lamp in combination with a grating monochromator., Comment: This paper has been withdrawn by the author due to the confusing layout in the whole article

Published
2014

14. [Prokaryotic expression and purification of N-terminal and C-terminal fragments of histone deacetylase 4].

Author

Yang Y, Qin XC, Liu SH, Huang W, and Wang XM

Subjects
Escherichia coli genetics, Escherichia coli metabolism, Glutathione Transferase biosynthesis, Glutathione Transferase genetics, Histone Deacetylases genetics, Humans, Peptide Fragments, Recombinant Fusion Proteins biosynthesis, Recombinant Fusion Proteins genetics, Repressor Proteins genetics, Genetic Vectors genetics, Histone Deacetylases biosynthesis, Recombinant Fusion Proteins isolation & purification, Repressor Proteins biosynthesis
Abstract

Objective: To express and purify the fusion proteins of glutathione S-transferase (GST)-N-terminal of histone deacetylase4 (HDAC4-N') (1-1952 bp) and GST- C-terminal of HDAC4 (HDAC4-C') (1708-3255 bp) in E.coli., Methods: The DNA fragments (HDAC4-N' and HDAC4-C') amplified by PCR were ligated into GST fusion vector (pGEX-6P-1) to construct the recombinant plasmids. After identification with restriction digestion and DNA sequencing, the recombinant plasmids were transformed into E.coli BL21 and induced by IPTG for their expression. After identification by SDS-PAGE and Western blotting, the target proteins were purified by glutathione sepharose 4B., Results: The results of restriction digestion and DNA sequencing confirmed successful construction of the recombinant plasmids. The relative molecular masses of the fusion proteins were approximately 110500 and 93080 as shown by SDS-PAGE. Western blotting demonstrated that the fusion proteins could be recognized by the specific anti-HDAC4 antibody., Conclusion: We have successfully constructed the recombinant expression vectors of pGEX-6P-1/HDAC4-N' and pGEX-6P-1/HDAC4-C' and induced the expression of the fusion proteins, which may facilitate functional studies of HDAC4 with other proteins.

Published
2010

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