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Crystallization and preliminary X‐ray diffraction analysis of Trap1 complexed with Hsp90 inhibitors
Author(s) -
Jeong Hanbin,
Kang Byoung Heon,
Lee Changwook
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14024959
Subject(s) - crystallography , hsp90 , crystallization , chemistry , molecule , x ray crystallography , diffraction , materials science , biochemistry , physics , optics , heat shock protein , organic chemistry , gene
Hsp90 is a molecular chaperone responsible for the assembly and regulation of many cellular client proteins. In particular, Trap1, a mitochondrial Hsp90 homologue, plays a pivotal role in maintaining mitochondrial integrity, protecting against apoptosis in cancer cells. The N (N‐terminal)‐M (middle) domain of human Trap1 was crystallized in complex with Hsp90 inhibitors (PU‐H71 and BIIB‐021) by the hanging‐drop vapour‐diffusion method at pH 6.5 and 293 K using 15% PEG 8K as a precipitant. Diffraction data were collected from crystals of the Trap1–PU‐H71 (2.7 Å) and Trap1–BIIB‐021 (3.1 Å) complexes to high resolution at a synchrotron‐radiation source. Preliminary X‐ray diffraction analysis revealed that both crystals belonged to space group P 4 1 2 1 2 or P 4 3 2 1 2, with unit‐cell parameters a = b = 69.2, c = 252.5 Å, and contained one molecule per asymmetric unit according to Matthews coefficient calculations.