Some notes on crystallizing fibrinogen and fibrin fragments

被引：6
|
作者：
Doolittle, RF [1 ]
机构：
[1] Univ Calif San Diego, Ctr Mol Genet, La Jolla, CA 92093 USA
来源：
BIOPHYSICAL CHEMISTRY | 2003年 / 100卷 / 1-3期
关键词：
fibrinogen; fibrin; crystal structures; trimethylamine oxide;
D O I：
10.1016/S0301-4622(02)00288-0
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
We have recently determined the structure of a native fibrinogen at 2.7-Angstrom resolution. Not the least of the hurdles during the many years of this project was growing X-ray-grade crystals from suitably purified proteins. Small, synthetic peptides based on the parts of fibrinogen exposed by the action of thrombin contributed greatly to these experiments. In addition, trimethylamine oxide (TMAO) was found to improve the diffraction of fibrinogen crystals. The history of my interest in fibrinogen and its crystallization can be traced back in part to some early interactions with John Edsall. (C) 2002 Elsevier Science B.V. All rights reserved.
引用
收藏
页码：307 / 313
页数：7
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