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Arabidopsis receptor-like cytoplasmic kinase BIK1: purification, crystallization and X-ray diffraction analysis.
- Source :
-
Acta crystallographica. Section F, Structural biology communications [Acta Crystallogr F Struct Biol Commun] 2016 Oct 01; Vol. 72 (Pt 10), pp. 738-742. Date of Electronic Publication: 2016 Sep 22. - Publication Year :
- 2016
-
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 C2, with two monomers per asymmetric unit.
- Subjects :
- Amino Acid Sequence
Arabidopsis enzymology
Arabidopsis immunology
Arabidopsis Proteins genetics
Arabidopsis Proteins immunology
Cloning, Molecular
Crystallization
Crystallography, X-Ray
Escherichia coli genetics
Escherichia coli metabolism
Gene Expression
Plasmids chemistry
Plasmids metabolism
Protein Serine-Threonine Kinases genetics
Protein Serine-Threonine Kinases immunology
Recombinant Proteins chemistry
Recombinant Proteins genetics
Recombinant Proteins immunology
X-Ray Diffraction
Arabidopsis chemistry
Arabidopsis Proteins chemistry
Protein Serine-Threonine Kinases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 2053-230X
- Volume :
- 72
- Issue :
- Pt 10
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology communications
- Publication Type :
- Academic Journal
- Accession number :
- 27710938
- Full Text :
- https://doi.org/10.1107/S2053230X16013522