来自人类病原体鼠伤寒沙门氏菌的甘油脱氢酶的结晶及初步X射线表征
Crystallization and preliminary X-ray characterization of a glycerol dehydrogenase from the human pathogen Salmonella enterica serovar Typhimurium.
作者信息
Gonçalves A T, Marçal D, Carrondo M A, Enguita F J
机构信息
Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, 2781-901 Oeiras, Portugal.
出版信息
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Jul 1;65(Pt 7):698-701. doi: 10.1107/S1744309109020296. Epub 2009 Jun 27.
Abstract
Glycerol dehydrogenase (GldA) encoded by the STM4108 gene (gldA) has been related to the synthesis of HilA, a major transcriptional regulator that is responsible for the expression of invasion genes in the human pathogen Salmonella enterica serovar Typhimurium. Single colourless crystals were obtained from a recombinant preparation of GldA overexpressed in Escherichia coli. They belonged to space group P222(1), with unit-cell parameters a = 127.0, b = 160.1, c = 665.2 A. The crystals contained a very large number of molecules in the asymmetric unit, probably 30-35. Diffraction data were collected to 3.5 A resolution using synchrotron radiation at the European Synchrotron Radiation Facility.
摘要
由STM4108基因（gldA）编码的甘油脱氢酶（GldA）与HilA的合成有关，HilA是一种主要的转录调节因子，负责人类病原体鼠伤寒沙门氏菌中侵袭基因的表达。从在大肠杆菌中过表达的GldA重组制剂中获得了无色单晶。它们属于空间群P222(1)，晶胞参数为a = 127.0、b = 160.1、c = 665.2 Å。不对称单元中的晶体包含大量分子，可能为30 - 35个。使用欧洲同步辐射装置的同步辐射将衍射数据收集至3.5 Å分辨率。
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