Crystallization and preliminary X-ray diffraction analysis of YidC, a membrane-protein chaperone and insertase from Bacillus halodurans

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.

Source: Acta Crystallographica Section F - July 23, 2014 Category: Biochemistry Authors: Kumazaki, K.Tsukazaki, T.Nishizawa, T.Tanaka, Y.Kato, H.E.Nakada-Nakura, Y.Hirata, K.Mori, Y.Suga, H.Dohmae, N.Ishitani, R.Nureki, O. Tags: YidC membrane-protein insertase lipidic cubic phase Bacillus halodurans crystallization communications Source Type: research