Effects of crystal twinning on the ability to solve a macromolecular structure using multiwavelength anomalous diffraction

被引：31

作者：

Yang, F

Dauter, Z

Wlodawer, A ^{[1
]}

机构：

[1] NCI, Prot Struct Sec, Macromol Crystallog Lab, Program Struct Biol,FCRDC, Frederick, MD 21702 USA

[2] Brookhaven Natl Lab, NSLS, Upton, NY 11973 USA

[3] NCI, Synchrotron Radiat Res Sect, Macromol Crystallog Lab, Program Struct Biol, Upton, NY 11973 USA

来源：

ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷

关键词：

D O I：

10.1107/S0907444900007162

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

The crystal structure of gpD, the capsid-stabilizing protein of bacteriophage lambda, was solved by multiwavelength anomalous diffraction (MAD) for a selenomethionine (SeMet) derivative of the protein at 1.8 Angstrom resolution, using crystals in space group P2(1) [Yang et al. (2000), Nature Struct. Biol. 7, 230-237]. Subsequent analysis showed that the crystals of both the original protein and the SeMet derivative were pseudomerohedrally twinned with a twinning fraction similar or equal to 0.36, owing to the near-identity of the a and c axes. An analysis of the crystal structure solution is presented and the utility of twinned crystals for solving the structure using MAD and of different phasing strategies is discussed; the results obtained with several software packages are compared.

引用

页码：959 / 964

页数：6

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[1] THE CCP4 SUITE - PROGRAMS FOR PROTEIN CRYSTALLOGRAPHY [J].