Crystallization and preliminary X-ray crystallographic analysis of the Hsp100 chaperone ClpB from Thermus thermophilus.

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Citation

Lee S, Hisayoshi M, Yoshida M, Tsai FT

Crystallization and preliminary X-ray crystallographic analysis of the Hsp100 chaperone ClpB from Thermus thermophilus.

Acta Crystallogr D Biol Crystallogr. 2003 Dec;59(Pt 12):2334-6. Epub 2003 Nov 27.

PubMed ID
14646112 [ View in PubMed
]
Abstract

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.

DrugBank Data that Cites this Article

Polypeptides
NameUniProt ID
Chaperone protein ClpBQ9RA63Details