X-ray diffraction analysis of a crystal of HscA from Escherichia coli.
X-ray diffraction analysis of a crystal of HscA from Escherichia coli.
复制标题
来自大肠杆菌的 HscA 晶体的 X 射线衍射分析。
DOI：
10.1107/s1744309105019251
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发表时间：
2005
期刊：
影响因子：
--
通讯作者：
Vickery,LarryE
中科院分区：
文献类型：
--
作者：
Aoto,PhillipC;Ta,DennisT;Cupp-Vickery,JillR;Vickery,LarryE
HscA is a constitutively expressed Hsp70 that interacts with the iron–sulfur cluster assembly protein IscU. Crystals of a truncated form of HscA (52 kDa; residues 17–505) grown in the presence of an IscU-recognition peptide, WELPPVKI, have been obtained by hanging-drop vapor diffusion using ammonium sulfate as the precipitant. A complete native X-ray diffraction data set was collected from a single crystal at 100 K to a resolution of 2.9 Å. The crystal belongs to the orthorhombic space group P212121, with unit-cell parameters a = 158.35, b = 166.15, c = 168.26 Å, and contains six molecules per asymmetric unit. Phases were determined by molecular replacement using the nucleotide-binding domain from DnaK and the substrate-binding domain from HscA as models. This is the first reported crystallization of an Hsp70 containing both nucleotide- and substrate-binding domains.
影响因子：
5.6
作者：
Morshauser, RC;Hu, WD;Zuiderweg, ERP
通讯作者：
Zuiderweg, ERP
影响因子：
5.6
作者：
Cupp-Vickery, JR;Peterson, JC;Vickery, LE
通讯作者：
Vickery, LE