Crystallization and preliminary X-ray analysis of the 9 kDa protein of the mouse signal recognition particle and the selenomethionyl-SRP9

被引：47

作者：

Doublie, S

Kapp, U

Aberg, A

Brown, K

Strub, K

Cusack, S

机构：

[1] INST MAX VON LAUE PAUL LANGEVIN, EUROPEAN MOLEC BIOL LAB, F-38042 GRENOBLE, FRANCE

[2] UNIV GENEVA, DEPT BIOL CELLULAIRE, CH-1211 GENEVA 4, SWITZERLAND

来源：

FEBS LETTERS | 1996年 / 384卷 / 03期

关键词：

signal recognition particle; incomplete factorial design; selenomethionyl protein; crystallization; X-ray diffraction;

D O I：

10.1016/0014-5793(96)00316-X

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：

Two different crystal forms of the 9 kDa protein of the signal recognition particle (SRP9) have been prepared by the hanging drop vapor diffusion technique using 28% (w/v) PEG8000 or 28% saturated ammonium sulphate as precipitant. The crystals are hexagonal bipyramids with average dimensions of 0.2 x 0.1 x 0.1 mm(3) and they diffract to a resolution of 2.3 Angstrom. They belong to the space groups P6(2)22/P6(4)22 or P3(1)21/P3(2)2 with cell dimensions a = b = 63.0 Angstrom, and c = 111.5 Angstrom. Crystals have also been grown from the selenomethionyl protein and multiwavelength data sets have been collected.

引用

页码：219 / 221

页数：3

共 11 条

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