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Crystallization and preliminary X‐ray diffraction analysis of YidC, a membrane‐protein chaperone and insertase from Bacillus halodurans
Author(s) -
Kumazaki Kaoru,
Tsukazaki Tomoya,
Nishizawa Tomohiro,
Tanaka Yoshiki,
Kato Hideaki E.,
NakadaNakura Yoshiko,
Hirata Kunio,
Mori Yoshihiro,
Suga Hiroaki,
Dohmae Naoshi,
Ishitani Ryuichiro,
Nureki Osamu
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/s2053230x14012540
Subject(s) - membrane protein , crystallography , transmembrane protein , chaperone (clinical) , membrane , chemistry , crystallization , biophysics , biology , biochemistry , receptor , medicine , organic chemistry , pathology
YidC, a member of the YidC/Oxa1/Alb3 family, inserts proteins into the membrane and facilitates membrane‐protein folding in bacteria. YidC plays key roles in both Sec‐mediated integration and Sec‐independent insertion of membrane proteins. Here, Bacillus halodurans YidC2, which has five transmembrane helices conserved among the other family members, was identified as a target protein for structure determination by a fluorescent size‐exclusion chromatography analysis. The protein was overexpressed, purified and crystallized in the lipidic cubic phase. The crystals diffracted X‐rays to 2.4 Å resolution and belonged to space group P 2 1 , with unit‐cell parameters a = 43.9, b = 60.6, c = 58.9 Å, β = 100.3°. The experimental phases were determined by the multiwavelength anomalous diffraction method using a mercury‐derivatized crystal.