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Expression, purification and preliminary crystallographic studies of the C‐terminal SH3 domain of human Tks4
Author(s) -
Huang Yuxin,
Qian Huolian,
Wang Xiaoying,
Cheng Zhong,
Ren Jixia,
Zhao Weichen,
Xie Yong
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x14001952
Subject(s) - sh3 domain , crystallography , resolution (logic) , homology (biology) , domain (mathematical analysis) , molecule , chemistry , c terminus , multiple isomorphous replacement , crystal (programming language) , proto oncogene tyrosine protein kinase src , diffraction , amino acid , stereochemistry , x ray crystallography , physics , mathematics , biochemistry , optics , computer science , mathematical analysis , organic chemistry , kinase , artificial intelligence , programming language
The Src homology 3 (SH3) domain is a small, noncatalytic domain with a conserved sequence of about 60 amino‐acid residues that interacts with proline‐rich peptides to form a protein complex. In this study, the C‐terminal SH3 domain of human Tks4 (residues 853–911) was expressed, purified and crystallized. X‐ray diffraction data were collected to 2.3 Å resolution. The crystal belonged to the trigonal space group P 3 1 21 (or P 3 2 21), with unit‐cell parameters a = b = 83.87, c = 108.44 Å, α = β = 90, γ = 120°. Calculating the self‐rotation and the native Patterson function did not lead to the detection of any noncrystallographic translational symmetry. Six, seven or eight protein molecules are likely to be present in the asymmetric unit, resulting in a Matthews coefficient and approximate solvent content of 2.71 Å 3 Da −1 and 55%, 2.32 Å 3 Da −1 and 47%, and 2.03 Å 3 Da −1 and 39%, respectively. To solve the crystal structure of the C‐terminal SH3 domain of human Tks4, the isomorphous replacement method is presently being utilized.