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结核分枝杆菌天冬氨酸半醛脱氢酶（Rv3708c）的纯化、结晶及初步X射线衍射分析

Purification, crystallization and preliminary X-ray diffraction analysis of aspartate semialdehyde dehydrogenase (Rv3708c) from Mycobacterium tuberculosis.

作者信息

Vyas Rajan, Kumar Vijay, Panjikar Santosh, Karthikeyan Subramanian, Kishan K V Radha, Tewari Rupinder, Weiss Manfred S

机构信息

Department of Biotechnology, Panjab University, Chandigarh 160 014, India.

出版信息

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Mar 1;64(Pt 3):167-70. doi: 10.1107/S1744309108002753. Epub 2008 Feb 23.

DOI:10.1107/S1744309108002753
PMID:18323599
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2374159/
Abstract

Aspartate semialdehyde dehydrogenase from Mycobacterium tuberculosis (Asd, ASADH, Rv3708c), which is the second enzyme in the lysine/homoserine-biosynthetic pathways, has been expressed heterologously in Escherichia coli. The enzyme was purified using affinity and gel-filtration chromatographic techniques and crystallized in two different crystal forms. Preliminary diffraction data analysis suggested the presence of up to four monomers in the asymmetric unit of the orthorhombic crystal form A and of one or two monomers in the cubic crystal form B.

摘要

来自结核分枝杆菌的天冬氨酸半醛脱氢酶（Asd、ASADH、Rv3708c）是赖氨酸/高丝氨酸生物合成途径中的第二种酶，已在大肠杆菌中进行了异源表达。该酶通过亲和色谱和凝胶过滤色谱技术进行纯化，并以两种不同的晶体形式结晶。初步衍射数据分析表明，在正交晶型A的不对称单元中最多存在四个单体，在立方晶型B中存在一个或两个单体。

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