A crystal of a typical EF-hand protein grown under microgravity diffracts X-rays beyond 0.9 Å resolution

被引：18

作者：

Declercq, JP

Evrard, C

Carter, DC

Wright, BS

Etienne, G

Parello, J

机构：

[1] Univ Catholique Louvain, Unite CPMC, B-1348 Louvain, Belgium

[2] New Century Pharmaceut Inc, Huntsville, AL 35824 USA

[3] Fac Pharm Montpellier, UPRESA, 5074 CNRS, F-34060 Montpellier, France

[4] Burnham Inst, La Jolla, CA 92037 USA

来源：

JOURNAL OF CRYSTAL GROWTH | 1999年 / 196卷 / 2-4期

基金：

美国国家航空航天局;

关键词：

protein crystallization; microgravity; atomic resolution; parvalbumin; calcium binding protein;

D O I：

10.1016/S0022-0248(98)00829-X

中图分类号：

O7 [晶体学];

学科分类号：

0702 ; 070205 ; 0703 ; 080501 ;

摘要：

We report on our recent observation that crystals of a typical EF-hand protein (parvalbumin or Pa; Ca-loaded component from pike muscle with isoelectric point 4.10) grown under microgravity conditions diffract X-rays to a resolution better than 0.9 Angstrom. The crystals were grown in the US space shuttle and characterized at 100 K, using an X-ray synchrotron beam. An effective atomic resolution has been achieved and substates in the conformation of the protein are observed. Large crystals up to 3 mm were also obtained. (C) 1999 Elsevier Science B.V. All rights reserved.

引用

页码：595 / 601

页数：7

共 20 条

[1] PROTEIN DATA BANK - COMPUTER-BASED ARCHIVAL FILE FOR MACROMOLECULAR STRUCTURES [J].