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Processing of X-ray diffraction data collected in oscillation mode.振荡模式下收集的X射线衍射数据的处理。
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Crystallization and preliminary X-ray analysis of the primary receptor (PotD) of the polyamine transport system in Escherichia coli.大肠杆菌中多胺转运系统初级受体(PotD)的结晶及初步X射线分析。
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Functional analysis and regulation of the divergent spuABCDEFGH-spuI operons for polyamine uptake and utilization in Pseudomonas aeruginosa PAO1.铜绿假单胞菌PAO1中用于多胺摄取和利用的发散型spuABCDEFGH-spuI操纵子的功能分析与调控
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大肠杆菌亚精胺乙酰转移酶的表达、纯化、结晶及初步晶体学分析

Expression, purification, crystallization and preliminary crystallographic analysis of spermidine acetyltransferase from Escherichia coli.

作者信息

Niiyama Mayumi, Sugiyama Shigeru, Hirose Mika, Ishikawa Sae, Tomitori Hideyuki, Higashi Kyohei, Yamashita Tomoko, Adachi Hiroaki, Takano Kazufumi, Murakami Satoshi, Murata Michio, Inoue Tsuyoshi, Mori Yusuke, Kashiwagi Keiko, Matsumura Hiroyoshi, Igarashi Kazuei

机构信息

Graduate School of Science, Osaka University, Suita, Osaka 565-0871, Japan.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Aug;69(Pt 8):884-7. doi: 10.1107/S1744309113017132. Epub 2013 Jul 27.

DOI:10.1107/S1744309113017132
PMID:23908034
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3729165/
Abstract

The spermidine acetyltransferase (SAT) from Escherichia coli catalyses the transfer of acetyl groups from acetyl-CoA to spermidine. SAT has been expressed and purified from E. coli. SAT was crystallized by the sitting-drop vapour-diffusion method to obtain a more detailed insight into the molecular mechanism. Preliminary X-ray diffraction studies revealed that the crystals diffracted to 2.5 Å resolution and belonged to the cubic space group P23, with unit-cell parameters a = b = c = 148.7 Å. They contained four molecules per asymmetric unit.

摘要

来自大肠杆菌的亚精胺乙酰转移酶(SAT)催化乙酰基从乙酰辅酶A转移至亚精胺。SAT已在大肠杆菌中表达并纯化。通过坐滴气相扩散法使SAT结晶,以更深入了解其分子机制。初步X射线衍射研究表明,晶体衍射分辨率达2.5 Å,属于立方晶系空间群P23,晶胞参数a = b = c = 148.7 Å。每个不对称单元包含四个分子。