title: Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the SH3 domain of human AHI1.
abstract: 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 A resolution at 110 K. The crystal belonged to space group P4(1)2(1)2, with unit-cell parameters a = 67.377, b = 67.377, c = 98.549 A.
authors.affiliation: Guangzhou Institute of Biomedicine and Health, Chinese Academy of Sciences, People's Republic of China.
authors.forename: Zhuliang
authors.initials: Z
authors.lastname: Shi
authors.forename: Ning
authors.initials: N
authors.lastname: Liang
authors.forename: Wei
authors.initials: W
authors.lastname: Xu
authors.forename: Kuai
authors.initials: K
authors.lastname: Li
authors.forename: Guoqing
authors.initials: G
authors.lastname: Sheng
authors.forename: Jinsong
authors.initials: J
authors.lastname: Liu
authors.forename: Aimin
authors.initials: A
authors.lastname: Xu
authors.forename: Xiao Jiang
authors.initials: XJ
authors.lastname: Li
authors.forename: Donghai
authors.initials: D
authors.lastname: Wu