Crystallization and preliminary X-ray crystallographic analysis of the Hsp100 chaperone ClpB from Thermus thermophilus.
ClpB from Thermus thermophilus (TClpB) has been crystallized by the vapour-diffusion method in the presence of adenosine 5'-(beta,gamma-imido)triphosphate (AMPPNP) and adenosine 5'-(gamma-thio)triphosphate (ATPgammaS), respectively. Complete native data sets have been collected from frozen crystals, which belonged to the primitive orthorhombic space group P2(1)2(1)2(1) with unit-cell parameters a = 109.2, b = 139.6, c = 213.0 A, alpha = beta = gamma = 90 degrees.
Lee
Sukyeong
S
Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, Houston, TX, USA.
Hisayoshi
Makyio
M
Yoshida
Masasuke
M
Tsai
Francis T F
FT
D001426:Bacterial Proteins / Q000737:chemistry* / Q000235:genetics; D003460:Crystallization; D018360:Crystallography, X-Ray; D001330:Electronic Data Processing; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000235:genetics; D018832:Molecular Chaperones / Q000737:chemistry* / Q000235:genetics; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000235:genetics / Q000378:metabolism; D016963:Thermus thermophilus / Q000737:chemistry*
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011994:Recombinant Proteins