Literature DB >> 24637764

Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the LRR domain of the LePRK1 receptor-like kinase from tomato.

Anbi Xu1, Laiqiang Huang2.   

Abstract

LePRK1 is a receptor-like kinase involved in successful fertilization in Lycopersicon esculentum (tomato). Importantly, the extracellular leucine-rich repeat (LRR) domain of LePRK1 mediates transmembrane signal transduction for pollen-tube growth and pollen germination. In this study, the N-terminal extracellular LRR domain of L. esculentum-derived LePRK1 was purified using an insect-cell secretion expression system and was crystallized by the vapour-diffusion method. The crystals diffracted X-rays to a resolution of 2.75 Å using synchrotron radiation. The crystals belonged to space group C2, with unit-cell parameters a = 136.53, b = 56.01, c = 62.93 Å, β = 108.99° and two molecules per asymmetric unit.

Entities:  

Keywords:  LRR; LePRK1; Lycopersicon esculentum; receptor-like kinases

Mesh:

Substances:

Year:  2014        PMID: 24637764      PMCID: PMC3936445          DOI: 10.1107/S2053230X13035024

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


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