Arabidopsis receptor‐like cytoplasmic kinase BIK1: purification, crystallization and X‐ray diffraction analysis. Issue 10 (6th October 2016)

• Record Type: Journal Article
• Authors: Lal, Neeraj K.; Fisher, Andrew J.; Dinesh-Kumar, Savithramma P.
• Is Part Of: Acta crystallographica. Volume 72:Issue 10(2016:Oct.)
• Page Start: 738
• Page End: 742
• Publication Date: 2016-10-06
• Subjects: receptor‐like kinase -- receptor‐like cytoplasmic kinases -- RLCK -- BIK1 -- BOTRYTIS‐INDUCED KINASE 1 -- PAMP‐triggered immunity -- Arabidopsis; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X16013522
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : The purification, crystallization and X‐ray diffraction analysis of the Arabidopsis receptor‐like cytoplasmic kinase BIK1, which plays an important role in growth and immune signaling pathways, are described. Abstract : Receptor‐like cytoplasmic kinases (RLCKs) in Arabidopsis play a central role in the integration of signaling input from various growth and immune signaling pathways. BOTRYTIS‐INDUCED KINASE 1 (BIK1), belonging to the RLCK family, is an important player in defense against bacterial and fungal pathogens and in ethylene and brassinosteroid hormone signaling. In this study, the purification and crystallization of a first member of the class VI family of RLCK proteins, BIK1, are reported. BIK1 was crystallized using the microbatch‐under‐oil method. X‐ray diffraction data were collected to 2.35 Å resolution. The crystals belonged to the monoclinic space group C 2, with two monomers per asymmetric unit.