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首页> 外文期刊>Acta crystallographica.Section D. Biological crystallography >Crystallization and preliminary X-ray crystallographic studies of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae.
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Crystallization and preliminary X-ray crystallographic studies of 3-deoxy-manno-octulosonate cytidylyltransferase from Haemophilus influenzae.

机译：结晶和初步的x射线晶体的研究流感嗜血杆菌。

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摘要

The enzyme 3-deoxy-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase; CKS) catalyzes the activation of 3-deoxy-manno-octulosonate (KDO) by forming CMP-KDO. It is essential for the biosynthesis of lipopolysaccharides in Gram-negative bacteria and is a potential target for the discovery of antibacterial agents. L-CKS from Haemophilus influenzae was overexpressed with a C-terminal hexahistidine tag in Escherichia coli and crystallized in the presence of the substrate KDO at 297 K using PEG 4000 as a precipitant and ethylene glycol as an additive. The diffraction limit and spot shape of the native crystal could be improved significantly by dehydration/annealing. X-ray diffraction data were collected to 2.5 A resolution from a native crystal. The crystals are orthorhombic, belonging to the space group P2(1)2(1)2(1), with unit-cell parameters a = 48.6, b = 83.1, c = 117.3 A. The presence of two monomers of recombinant L-CKS in the crystallographic asymmetric unit gives a reasonable V(M) of 2.05 A(3) Da(-1), with a solvent content of 40.0%.
机译：这种酶3-deoxy-manno-octulosonatecytidylyltransferase (CMP-KDO合成酶;催化的激活3-deoxy-manno-octulosonate (KDO)形成CMP-KDO。在革兰氏阴性细菌和脂多糖是一个潜在的目标的发现抗菌药物。流感嗜血杆菌是过表达c端在大肠杆菌和hexahistidine标签固定在衬底KDO的存在在297 K使用4000作为沉淀剂和挂钩乙二醇作为添加剂。限制和现货原生晶体的形状明显改善的脱水/退火。从本地收集到2.5决议晶体。空间群P2(1) 2(1) 2(1),与单胞参数= 48.6,b = 83.1, c = 117.3。两个重组L-CKS单体的存在晶体不对称单位了合理的2.05 V (M) (3) Da(1),和一个溶剂含量的40.0%。

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