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硫的异常信号能否成为解析蛋白质晶体结构的工具?

Can anomalous signal of sulfur become a tool for solving protein crystal structures?

作者信息

Dauter Z, Dauter M, de La Fortelle E, Bricogne G, Sheldrick G M

机构信息

National Cancer Institute, Frederick and Brookhaven National Laboratory, Building 725A-X9, Upton, NY, 11973, USA.

出版信息

J Mol Biol. 1999 May 28;289(1):83-92. doi: 10.1006/jmbi.1999.2743.

DOI:10.1006/jmbi.1999.2743
PMID:10339407
Abstract

A general method for solving the phase problem from native crystals of macromolecules has long eluded structural biology. For well diffracting crystals this goal can now be achieved, as is shown here, thanks to modern data collection techniques and new statistical phasing algorithms. Using solely a native crystal of tetragonal hen egg-white lysozyme, a protein of 14 kDa molecular mass, it was possible to detect the positions of the ten sulfur and seven chlorine atoms from their anomalous signal, and proceed from there to obtain an electron-density map of very high quality.

摘要

长期以来,结构生物学一直未能找到一种从大分子天然晶体中解决相位问题的通用方法。正如本文所示,借助现代数据收集技术和新的统计相位算法,对于衍射良好的晶体,现在可以实现这一目标。仅使用四方晶系的鸡蛋清溶菌酶(一种分子量为14 kDa的蛋白质)的天然晶体,就有可能从其反常信号中检测到十个硫原子和七个氯原子的位置,并在此基础上获得高质量的电子密度图。

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