正交晶系
结晶学
大肠杆菌
单体
结晶
化学
二聚体
晶体结构
转移RNA
摆动碱基对
GTP酶
立体化学
基因
生物化学
核糖核酸
聚合物
有机化学
作者
Hyung Ho Lee,Se Won Suh
出处
期刊:Acta crystallographica
[International Union of Crystallography]
日期:2010-07-27
卷期号:66 (8): 905-908
标识
DOI:10.1107/s1744309110018750
摘要
MnmE, an evolutionarily conserved GTPase, is involved in modification of the uridine base (U34) at the wobble position of certain tRNAs. Previous crystal structures of MnmE suggest that it is a dimer with considerable conformational flexibility. To facilitate structural comparisons among MnmE proteins, structural analysis of MnmE from Pseudomonas aeruginosa encoded by the PA5567 gene was initiated. It was overexpressed in Escherichia coli and crystallized at 297 K using a reservoir solution consisting of 100 mM sodium ADA pH 6.5, 12%(w/v) polyethylene glycol 4000, 100 mM lithium sulfate, 2%(v/v) 2-propanol and 2.5 mM dithiothreitol. X-ray diffraction data were collected to 2.69 A resolution. The crystals belonged to the orthorhombic space group C222(1), with unit-cell parameters a=96.74, b=204.66, c=120.90 A. Two monomers were present in the asymmetric unit, resulting in a crystal volume per protein mass (VM) of 2.99 A3 Da(-1) and a solvent content of 58.8%.
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