title: Crystallization and preliminary crystallographic analysis of Arabidopsis thaliana BRI1-associated kinase 1 (BAK1) cytoplasmic domain.
abstract: 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 C2, 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).
authors.affiliation: Laboratory of Structural Biology, School of Medicine, Tsinghua University, Beijing 100084, People's Republic of China.
authors.forename: Jian
authors.initials: J
authors.lastname: Gao
authors.forename: Yuanyuan
authors.initials: Y
authors.lastname: Ma
authors.forename: Yuna
authors.initials: Y
authors.lastname: Sun
authors.forename: Huadong
authors.initials: H
authors.lastname: Zhao
authors.forename: Dapeng
authors.initials: D
authors.lastname: Hong
authors.forename: Liming
authors.initials: L
authors.lastname: Yan
authors.forename: Zhiyong
authors.initials: Z
authors.lastname: Lou
mesh_terms: D017360:Arabidopsis / Q000201:enzymology*; D029681:Arabidopsis Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D003593:Cytoplasm / Q000201:enzymology; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*
chemical_list: D029681:Arabidopsis Proteins; C463660:BAK1 protein, Arabidopsis; D017346:Protein Serine-Threonine Kinases