The purification and preliminary crystallographic analysis of the archaeal CBS-domain protein MJ1004 from Methanocaldococcus jannaschii are described. The native protein was overexpressed, purified and crystallized in the monoclinic space group P2(1), with unit-cell parameters a=54.4, b=53.8, c=82.6â à , β=106.1°. The crystals diffracted X-rays to 2.7â à resolution using synchrotron radiation. Matthews-volume calculations suggested the presence of two molecules in the asymmetric unit that are likely to correspond to a dimeric species, which is also observed in solution.
Purification, crystallization and preliminary crystallographic analysis of the CBS-domain protein MJ1004 from Methanocaldococcus jannaschii.
阅读:6
作者:Oyenarte Iker, Lucas MarÃa, Gómez GarcÃa Inmaculada, MartÃnez-Cruz Luis Alfonso
| 期刊: | Acta Crystallographica Section F-Structural Biology and Crystallization Communications | 影响因子: | 1.100 |
| 时间: | 2011 | 起止号: | 2011 Mar 1; 67(Pt 3):318-24 |
| doi: | 10.1107/S1744309110053479 | ||
特别声明
1、本页面内容包含部分的内容是基于公开信息的合理引用;引用内容仅为补充信息,不代表本站立场。
2、若认为本页面引用内容涉及侵权,请及时与本站联系,我们将第一时间处理。
3、其他媒体/个人如需使用本页面原创内容,需注明“来源:[生知库]”并获得授权;使用引用内容的,需自行联系原作者获得许可。
4、投稿及合作请联系:info@biocloudy.com。
