Open AccessCrystallization and preliminary crystallographic analysis of Arabidopsis thaliana BRI1‐associated kinase 1 (BAK1) cytoplasmic domain
Author(s) -
Gao Jian,
Ma Yuanyuan,
Sun Yuna,
Zhao Huadong,
Hong Dapeng,
Yan Liming,
Lou Zhiyong
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309112004605
Subject(s) - protein kinase domain , brassinosteroid , kinase , arabidopsis thaliana , crystallography , arabidopsis , chemistry , domain (mathematical analysis) , biology , microbiology and biotechnology , biochemistry , gene , mutant , mathematical analysis , mathematics
BRI1‐associated kinase 1 (BAK1) is a member of the plant receptor‐like kinase (RLK) superfamily. BAK1 has been shown to initiate brassinosteroid (BR) signalling and innate immune responses in plants by forming receptor complexes with both brassinosteroid‐insensitive 1 (BRI1) and flagellin‐sensing 2 (FLS2). To gain a better understanding of the structural details and the mechanism of action of the BAK1 kinase domain, recombinant BAK1 cytoplasmic domain has been expressed, purified and crystallized at 291 K using PEG 3350 as a precipitant. A 2.6 Å resolution data set was collected from a single flash‐cooled crystal at 100 K. This crystal belonged to space group C 2, with unit‐cell parameters a = 70.3, b = 75.6, c = 71.9 Å, β = 93.1°. Assuming the presence of one molecule in the asymmetric unit, the Matthews coefficient was 2.6 Å 3 Da −1 .