Expression, purification and crystallization of a human protein SH3BGRL at atomic resolution.
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 A resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 28.8886, b = 34.9676, c = 98.0016 A. Preliminary analysis indicates that the asymmetric unit contains one molecule and has a solvent content of about 34%.
Yin
Lei
L
Center for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, People's Republic of China.
Zhu
De-Yu
DY
Yang
Na
N
Huang
Qiu-Hua
QH
Zhang
Ying
Y
Wang
Da-Cheng
DC
D003001:Cloning, Molecular; D003460:Crystallization / Q000379:methods; D006801:Humans; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D014835:Volatilization; D014961:X-Ray Diffraction; D018909:src Homology Domains
D011506:Proteins; C113099:SH3BGRL protein, human