Journal
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS
Volume 68, Issue -, Pages 340-342Publisher
INT UNION CRYSTALLOGRAPHY
DOI: 10.1107/S1744309112004605
Keywords
BRI1-associated kinase 1; receptor-like kinases; Arabidopsis thaliana
Funding
- National Natural Science Foundation of China [31000332, 31100208, 31170782]
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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 angstrom 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 angstrom, beta = 93.1 degrees. Assuming the presence of one molecule in the asymmetric unit, the Matthews coefficient was 2.6 angstrom 3 Da-1.
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