• 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

Expression, purification, crystallization and preliminary crystallographic analysis of osmotically inducible protein C.

作者信息

Rehse Peter H, Nodake Yuichi, Kuroishi Chizu, Tahirov Tahir H

机构信息

Highthroughput Factory, RIKEN Harima Institute, 1-1-1 Kouto, Mikazuki-cho, Sayo-gun, Hyogo 679-5148, Japan.

出版信息

Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):357-8. doi: 10.1107/S0907444903027458. Epub 2004 Jan 23.

DOI:10.1107/S0907444903027458
PMID:14747724
Abstract

Selenium-incorporated osmotically inducible protein C from the thermophilic bacterium Thermus thermophilus was overexpressed, purified and crystallized. The crystals belong to space group P1, with unit-cell parameters a = 37.58, b = 40.95, c = 48.14 A, alpha = 76.93, beta = 74.04, gamma = 64.05 degrees. Five data sets were collected from a single crystal to 1.6 A using synchrotron radiation for MAD phasing. Self-rotation functions and the Matthews coefficient are consistent with two molecules in the asymmetric unit.

摘要

相似文献

1
Expression, purification, crystallization and preliminary crystallographic analysis of osmotically inducible protein C.
Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):357-8. doi: 10.1107/S0907444903027458. Epub 2004 Jan 23.
2
Purification, crystallization, and preliminary X-ray crystallographic analysis of thermus thermophilus V(1)-ATPase B subunit.嗜热栖热菌V(1)-ATP酶B亚基的纯化、结晶及初步X射线晶体学分析
J Struct Biol. 1999 Aug;127(1):79-82. doi: 10.1006/jsbi.1999.4140.
3
Crystallographic structure and biochemical analysis of the Thermus thermophilus osmotically inducible protein C.嗜热栖热菌渗透压诱导蛋白C的晶体结构及生化分析
J Mol Biol. 2004 May 14;338(5):959-68. doi: 10.1016/j.jmb.2004.03.050.
4
Expression, purification and preliminary crystallographic analysis of dipeptidyl peptidase IV from Porphyromonas gingivalis.牙龈卟啉单胞菌二肽基肽酶IV的表达、纯化及初步晶体学分析
Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1871-3. doi: 10.1107/S0907444904017639. Epub 2004 Sep 23.
5
Crystallization and preliminary X-ray crystallographic analysis of peptide deformylase from Thermus thermophilus HB8.嗜热栖热菌HB8肽脱甲酰基酶的结晶及初步X射线晶体学分析
Acta Crystallogr D Biol Crystallogr. 2004 Jul;60(Pt 7):1299-300. doi: 10.1107/S0907444904010595. Epub 2004 Jun 22.
6
Crystallization and preliminary X-ray analysis of carboxypeptidase 1 from Thermus thermophilus.嗜热栖热菌羧肽酶1的结晶及初步X射线分析
Acta Crystallogr D Biol Crystallogr. 2004 Aug;60(Pt 8):1445-6. doi: 10.1107/S0907444904012557. Epub 2004 Jul 21.
7
Crystallization and preliminary X-ray crystallographic study of leucyl-tRNA synthetase from the archaeon Pyrococcus horikoshii.嗜热栖热袍菌亮氨酰-tRNA合成酶的结晶及初步X射线晶体学研究
Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1916-8. doi: 10.1107/S0907444904020700. Epub 2004 Sep 23.
8
Crystallization and preliminary X-ray crystallographic analysis of a ytfG gene product from Escherichia coli.来自大肠杆菌的ytfG基因产物的结晶及初步X射线晶体学分析
Acta Crystallogr D Biol Crystallogr. 2004 Feb;60(Pt 2):365-7. doi: 10.1107/S0907444903027781. Epub 2004 Jan 23.
9
Crystallization and preliminary X-ray crystallographic study of the editing domain of Thermus thermophilus isoleucyl-tRNA synthetase complexed with pre- and post-transfer editing-substrate analogues.嗜热栖热菌异亮氨酰 - tRNA合成酶编辑结构域与转移前和转移后编辑底物类似物复合物的结晶及初步X射线晶体学研究。
Acta Crystallogr D Biol Crystallogr. 2004 Oct;60(Pt 10):1900-2. doi: 10.1107/S0907444904019511. Epub 2004 Sep 23.
10
Purification, crystallization and initial crystallographic analysis of RNA polymerase holoenzyme from Thermus thermophilus.嗜热栖热菌RNA聚合酶全酶的纯化、结晶及初步晶体学分析
Acta Crystallogr D Biol Crystallogr. 2002 Sep;58(Pt 9):1497-500. doi: 10.1107/S0907444902011770. Epub 2002 Aug 23.