• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

Preliminary X-ray crystallographic studies of photosynthetic reaction center from a thermophilic sulfur bacterium, Chromatium tepidum.

作者信息

Katayama N, Kobayashi M, Motojima F, Inaka K, Nozawa T, Miki K

机构信息

Research Laboratory of Resources Utilization, Tokyo Institute of Technology, Yokohama, Japan.

出版信息

FEBS Lett. 1994 Jul 11;348(2):158-60. doi: 10.1016/0014-5793(94)00534-6.

DOI:10.1016/0014-5793(94)00534-6
PMID:8034032
Abstract

A membrane protein complex, photosynthetic reaction center purified from the thermophilic purple sulfur bacterium, Chromatium tepidum has been crystallized from a phosphate buffer containing a detergent, n-octyl-beta-D-glucopyranoside and a precipitant, polyethylene glycol 4000. The crystals diffracted X-rays beyond 3A resolution with synchrotron radiation and are suitable for high-resolution X-ray crystallographic studies. The crystals belong to the orthorhombic space group P2(1)2(1)2(1) with unit-cell dimensions of a = 136A, b = 197A, and c = 82A. Assuming that they contain one reaction center complex in the asymmetric unit, VM was calculated to be 4.3 A3/Da, which agrees with the values obtained in the membrane protein complexes.

摘要

相似文献

1
Preliminary X-ray crystallographic studies of photosynthetic reaction center from a thermophilic sulfur bacterium, Chromatium tepidum.
FEBS Lett. 1994 Jul 11;348(2):158-60. doi: 10.1016/0014-5793(94)00534-6.
2
Crystallization and preliminary crystallographic analysis of the high-potential iron-sulfur protein from Thermochromatium tepidum.嗜热栖热菌高电位铁硫蛋白的结晶及初步晶体学分析
Acta Crystallogr D Biol Crystallogr. 2000 May;56(Pt 5):656-8. doi: 10.1107/s0907444900003127.
3
Crystallization of the reaction center from Rhodobacter sphaeroides in a new tetragonal form.
Proteins. 1994 Nov;20(3):283-6. doi: 10.1002/prot.340200309.
4
Purification and crystallization of the light harvesting LH1 complex from Rhodobacter sphaeroides.球形红细菌光捕获LH1复合物的纯化与结晶
J Mol Biol. 1992 Dec 20;228(4):1259-62. doi: 10.1016/0022-2836(92)90331-d.
5
Crystallization of two integral membrane pigment-protein complexes from the purple-sulfur bacterium Chromatium purpuratum.来自紫色硫细菌紫硫色杆菌的两种整合膜色素蛋白复合物的结晶。
Protein Sci. 1993 Aug;2(8):1352-5. doi: 10.1002/pro.5560020818.
6
Properties of the reaction center of the thermophilic purple photosynthetic bacterium Chromatium tepidum.
Biochim Biophys Acta. 1987 Dec 17;894(3):468-76. doi: 10.1016/0005-2728(87)90126-5.
7
Crystallization and the crystal properties of the oxygen-evolving photosystem II from Synechococcus vulcanus.嗜热栖热放线菌放氧光系统II的结晶及晶体性质
Biochemistry. 2000 Dec 5;39(48):14739-44. doi: 10.1021/bi001402m.
8
Crystallization and X-ray analysis of the reaction center from the thermophilic green bacterium Chloroflexus aurantiacus.嗜热绿菌橙色绿屈挠菌反应中心的结晶与X射线分析。
FEBS Lett. 1996 Nov 4;396(2-3):161-4. doi: 10.1016/0014-5793(96)01101-5.
9
Characterization of flavocytochrome C552 from the thermophilic photosynthetic bacterium Chromatium tepidum.嗜热光合细菌嗜温色杆菌中黄素细胞色素C552的特性研究。
Arch Biochem Biophys. 1994 Dec;315(2):262-6. doi: 10.1006/abbi.1994.1498.
10
Crystallization and preliminary X-ray diffraction analysis of the light-harvesting protein phycocyanin from the thermophilic cyanobacterium Synechococcus elongatus.嗜热蓝藻聚球藻中光捕获蛋白藻蓝蛋白的结晶及初步X射线衍射分析
Acta Crystallogr D Biol Crystallogr. 2001 Sep;57(Pt 9):1326-8. doi: 10.1107/s0907444901011969. Epub 2001 Aug 23.

引用本文的文献

1
Crystal structures of photosynthetic reaction center and high-potential iron-sulfur protein from Thermochromatium tepidum: thermostability and electron transfer.嗜热栖热菌光合反应中心和高电位铁硫蛋白的晶体结构:热稳定性与电子转移
Proc Natl Acad Sci U S A. 2000 Dec 5;97(25):13561-6. doi: 10.1073/pnas.240224997.