Reference - Detail
| RRC ID | 30929 |
|---|---|
| Author | Kumazaki K, Tsukazaki T, Nishizawa T, Tanaka Y, Kato HE, Nakada-Nakura Y, Hirata K, Mori Y, Suga H, Dohmae N, Ishitani R, Nureki O. |
| Title | Crystallization and preliminary X-ray diffraction analysis of YidC, a membrane-protein chaperone and insertase from Bacillus halodurans. |
| Journal | Acta Crystallogr F Struct Biol Commun |
| 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. |
| Volume | 70(Pt 8) |
| Pages | 1056-60 |
| Published | 2014-8-1 |
| DOI | 10.1107/S2053230X14012540 |
| PII | S2053230X14012540 |
| PMID | 25084381 |
| PMC | PMC4118803 |
| MeSH | Bacillus / chemistry* Bacillus / enzymology Bacterial Proteins / chemistry* Chromatography, Gel Crystallography, X-Ray Enzymes / chemistry* Molecular Chaperones / chemistry* |
| IF | 0.968 |
| Times Cited | 5 |
| WOS Category | CRYSTALLOGRAPHY BIOCHEMICAL RESEARCH METHODS BIOPHYSICS BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Altmetric score |
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| The most frequently cited source | X(Twitter) |
| Total number of mentions | 4 |
| Altmetric score changes over past 6months | 0.0 |
| Resource | |
| DNA material | Genomic DNA of Bacillus halodurans JCM 9153 (JGD12232) |
| General Microbes | |