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- Title
Crystallization and preliminary X-ray diffraction analysis of YidC, a membrane-protein chaperone and insertase from Bacillus halodurans.
- Authors
Kumazaki, Kaoru; Tsukazaki, Tomoya; Nishizawa, Tomohiro; Tanaka, Yoshiki; Kato, Hideaki E.; Nakada-Nakura, Yoshiko; Hirata, Kunio; Mori, Yoshihiro; Suga, Hiroaki; Dohmae, Naoshi; Ishitani, Ryuichiro; Nureki, Osamu
- Abstract
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 P21, 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.
- Subjects
X-ray diffraction; MEMBRANE proteins; BACILLUS halodurans; PROTEIN folding; CHROMATOGRAPHIC analysis; PROTEIN structure
- Publication
Acta Crystallographica: Section F, Structural Biology Communications, 2014, Vol 70, Issue 8, p1056
- ISSN
2053-230X
- Publication type
Article
- DOI
10.1107/S2053230X14012540