X-ray diffraction analysis of a crystal of HscA from Escherichia coli.

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 A. The crystal belongs to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 158.35, b = 166.15, c = 168.26 A, 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.

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