信号识别颗粒SRPphi14-9融合蛋白的结晶及初步晶体学分析

Crystallization and preliminary crystallographic analysis of the signal recognition particle SRPphi14-9 fusion protein.

作者信息

Birse D E, Doublié S, Kapp U, Strub K, Cusack S, Aberg A

机构信息

European Molecular Biology Laboratory, Grenoble Outstation, France.

出版信息

FEBS Lett. 1996 Apr 22;384(3):215-8. doi: 10.1016/0014-5793(96)00315-8.

DOI:10.1016/0014-5793(96)00315-8

PMID:8617356

Abstract

The SRPphi14-9 fusion protein, which can functionally replace the SRP9/14 heterodimer in the mammalian signal recognition particle (SRP), has been crystallized using the vapor diffusion method. Four different crystal forms were grown. SRPphi14-9 form IV crystals belong to the space group P4(1)22/ P4(3)22 with cell parameters a = b = 69.7 Angstroms, c = 95.7 Angstroms, alpha = beta = gamma = 90 degrees. A complete data set to 2.8 Angstroms resolution with an Rsym on intensities of 7.0% was collected on a single flash-frozen crystal.

摘要

能够在功能上替代哺乳动物信号识别颗粒（SRP）中的SRP9/14异二聚体的SRPphi14-9融合蛋白，已通过气相扩散法结晶。生长出了四种不同的晶体形式。SRPphi14-9 IV型晶体属于空间群P4(1)22/ P4(3)22，晶胞参数为a = b = 69.7埃，c = 95.7埃，α = β = γ = 90度。在一块单次快速冷冻的晶体上收集到了分辨率为2.8埃的完整数据集，强度的Rsym为7.0%。