Crystallization and preliminary X-ray diffraction studies of the guanylate kinase-like domain of PSD-95 protein from rat

被引:0
|
作者
Kim, JJ
Rho, SH
Im, YJ
Kim, EJ
Eom, SH [1 ]
机构
[1] Kwangju Inst Sci & Technol, Dept Life Sci, Kwangju 500712, South Korea
[2] Korea Adv Inst Sci & Technol, Dept Biol Sci, Taejon 305701, South Korea
关键词
D O I
10.1107/S0907444901001937
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
The PSD-95 (postsynaptic density-95) protein, one of the members of the MAGUK (membrane-associated guanylate kinase) family, is composed of three PDZ domains, one SH3 domain and one guanylate kinase-like (GK) domain. The GK domain mediates the scaffolding function of PSD-95 by protein-protein interaction. Here, the GK domain was subcloned, expressed as an intein fusion protein, purified without the intein and then crystallized at room temperature by the hanging-drop vapour-diffusion method using PEG 8000 as a precipitant. The complete native data set was collected to a resolution of 2.35 Angstrom using flash-cooling. The crystals belong to the primitive tetragonal space group P4(3) (or P4(1)), with unit-cell parameters a = b = 70.03 (4), c = 37.64 (1) Angstrom.
引用
收藏
页码:616 / 617
页数:2
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