Open AccessExpression, purification, crystallization and preliminary X‐ray crystallographic analysis of the SH3 domain of human AHI1
Author(s) -
Shi Zhuliang,
Liang Ning,
Xu Wei,
Li Kuai,
Sheng Guoqing,
Liu Jinsong,
Xu Aimin,
Li XiaoJiang,
Wu Donghai
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910900774x
Subject(s) - crystallization , crystallography , resolution (logic) , escherichia coli , crystal (programming language) , sh3 domain , domain (mathematical analysis) , materials science , chemistry , gene , biochemistry , receptor , mathematics , proto oncogene tyrosine protein kinase src , computer science , organic chemistry , artificial intelligence , programming language , mathematical analysis
The SH3 domain of human AHI1 was cloned and expressed in Escherichia coli . The protein was purified by affinity and size‐exclusion chromatography and was crystallized using the sitting‐drop vapour‐diffusion method at 293 K. A complete data set was collected to 2.5 Å resolution at 110 K. The crystal belonged to space group P 4 1 2 1 2, with unit‐cell parameters a = 67.377, b = 67.377, c = 98.549 Å.