Crystallization and preliminary X-ray crystallographic properties of Hsc20, a J-motif co-chaperone protein from Escherichia coli.
Crystallization and preliminary X-ray crystallographic properties of Hsc20, a J-motif co-chaperone protein from Escherichia coli.
复制标题
Hsc20（一种来自大肠杆菌的 J 基序辅助伴侣蛋白）的结晶和初步 X 射线晶体学特性。
DOI：
10.1002/pro.5560060923
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发表时间：
1997
期刊：
影响因子：
--
通讯作者：
Vickery,LE
中科院分区：
文献类型：
--
作者：
Cupp-Vickery,JR;Vickery,LE
Hsc20 is a 20‐kDa auxiliary protein that functions with the molecular chaperone Hsc66 inEscherichia coli.Crystals of Hsc20 suitable for X‐ray diffraction analysis were grown using the hanging drop vapor diffusion technique in polyethylene glycol 400 containing dioxane as an additive to slow growth. The crystals are monoclinic and belong to the space groupC2with unit cell dimensions α = 125.4 Å,b= 71.9 Å,c= 68.8 Å, and β = 97.0°. The crystals diffract to a minimumd‐spacing of ∼2.5 Å resolution, and a native data set was collected to 2.7 Å. The results of a self‐rotation function analysis revealed threefold symmetry, suggesting three molecules of Hsc20 in the asymmetric unit and, hence, 12 molecules in the unit cell; this corresponds to aVmvalue of 2.6 Å3/Da and a solvent content of ∼53% in the crystals. Structure determination by isomorphous replacement is in progress.
