Open AccessExpression, purification and crystallization of a human protein SH3BGRL at atomic resolution
Author(s) -
Yin Lei,
Zhu DeYu,
Yang Na,
Huang QiuHua,
Zhang Ying,
Wang DaCheng
Publication year - 2005
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910500730x
Subject(s) - crystallization , resolution (logic) , crystallography , solvent , molecule , materials science , high resolution , diffraction , drop (telecommunication) , chemistry , biochemistry , organic chemistry , optics , physics , remote sensing , telecommunications , artificial intelligence , computer science , geology
The protein SH3BGRL, containing both SH3‐binding and Homer EVH1‐binding motifs, has been crystallized using the hanging‐drop vapour‐diffusion method. The crystals diffract to 0.88 Å resolution and belong to space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 28.8886, b = 34.9676, c = 98.0016 Å. Preliminary analysis indicates that the asymmetric unit contains one molecule and has a solvent content of about 34%.