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Crystallization and preliminary X-ray diffraction analysis of the 10 kDa C-terminal subdomain of 70 kDa heat-shock cognate protein
Journal article   Peer reviewed

Crystallization and preliminary X-ray diffraction analysis of the 10 kDa C-terminal subdomain of 70 kDa heat-shock cognate protein

C.-C. Chou, C. Wang, Y.-J. Sun, H.-L. Shr and C.-D. Hsiao
Acta Crystallographica Section D: Biological Crystallography, Vol.57(12), pp.1928-1930
2001

Abstract

The 70 kDa heat-shock cognate protein (Hsc70) is a cytosolic molecular chaperone. It is composed of a 44 kDa N-terminal nucleotide-binding domain, an 18 kDa peptide-binding subdomain and a 10 kDa C-terminal subdomain. Single crystals of recombinant 10 kDa subdomain of rat Hsc70 have been obtained using ammonium sulfate as a precipitant at room temperature. The crystals diffract beyond 3.5 Å using a synchrotron-radiation source at a wavelength of 1.0 Å. The crystals belong to the hexagonal space group P6 1 22 or P6 5 22, with unit-cell parameters a = b = 119.0, c = 166.4 Å.

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