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嗜酸热原体转醛醇酶的结晶及初步X射线衍射分析

Crystallization and preliminary X-ray diffraction analysis of transaldolase from Thermoplasma acidophilum.

作者信息

Lehwess-Litzmann Anja, Neumann Piotr, Golbik Ralph, Parthier Christoph, Tittmann Kai

机构信息

Göttinger Zentrum für Molekulare Biowissenschaften, Georg-August-Universität Göttingen, Ernst-Caspari-Haus, Justus-von-Liebig-Weg 11, D-37077 Göttingen, Germany.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 May 1;67(Pt 5):584-6. doi: 10.1107/S1744309111009274. Epub 2011 Apr 27.

DOI:10.1107/S1744309111009274
PMID:21543867
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3087646/
Abstract

The metabolic enzyme transaldolase from Thermoplasma acidophilum was recombinantly expressed in Escherichia coli and could be crystallized in two polymorphic forms. Crystals were grown by the hanging-drop vapour-diffusion method using PEG 6000 as precipitant. Native data sets for crystal forms 1 and 2 were collected in-house to resolutions of 3.0 and 2.7 Å, respectively. Crystal form 1 belonged to the orthorhombic space group C222(1) with five monomers per asymmetric unit and crystal form 2 belonged to the monoclinic space group P2(1) with ten monomers per asymmetric unit.

摘要

嗜热栖热菌的代谢酶转醛醇酶在大肠杆菌中进行了重组表达，并能以两种多晶型形式结晶。使用聚乙二醇6000作为沉淀剂，通过悬滴气相扩散法生长晶体。内部收集了晶型1和晶型2的天然数据集，分辨率分别为3.0 Å和2.7 Å。晶型1属于正交晶系空间群C222(1)，每个不对称单元有五个单体，晶型2属于单斜晶系空间群P2(1)，每个不对称单元有十个单体。

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Crystal structure of transaldolase B from Escherichia coli suggests a circular permutation of the alpha/beta barrel within the class I aldolase family.来自大肠杆菌的转醛醇酶B的晶体结构表明I类醛缩酶家族中α/β桶状结构存在环状排列。
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