Crystallization and preliminary X-ray diffraction analysis of the 10 kDa C-terminal subdomain of 70 kDa heat-shock cognate protein.
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 A using a synchrotron-radiation source at a wavelength of 1.0 A. 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 A.
Chou
C C
CC
Institute of Molecular Biology, Academia Sinica, Taipei 115, Taiwan.
Wang
C
C
Sun
Y J
YJ
Shr
H L
HL
Hsiao
C D
CD
D000818:Animals; D003460:Crystallization; D018360:Crystallography, X-Ray; D050883:HSC70 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000737:chemistry*; D008970:Molecular Weight; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D051381:Rats
D050883:HSC70 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; C494373:Hspa8 protein, rat; D010446:Peptide Fragments