title: Expression, purification and crystallization of a human protein SH3BGRL at atomic resolution.
abstract: 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%.
authors.affiliation: Center for Structural and Molecular Biology, Institute of Biophysics, Chinese Academy of Science, Beijing 100101, People's Republic of China.
authors.forename: Lei
authors.initials: L
authors.lastname: Yin
authors.forename: De-Yu
authors.initials: DY
authors.lastname: Zhu
authors.forename: Na
authors.initials: N
authors.lastname: Yang
authors.forename: Qiu-Hua
authors.initials: QH
authors.lastname: Huang
authors.forename: Ying
authors.initials: Y
authors.lastname: Zhang
authors.forename: Da-Cheng
authors.initials: DC
authors.lastname: Wang
mesh_terms: 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
chemical_list: D011506:Proteins; C113099:SH3BGRL protein, human