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Cloning, expression, purification, crystallization and preliminary X‐ray diffraction analysis of the LRR domain of the LePRK1 receptor‐like kinase from tomato
Author(s) -
Xu Anbi,
Huang Laiqiang
Publication year - 2014
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x13035024
Subject(s) - extracellular , protein kinase domain , pollen tube , lycopersicon , leucine rich repeat , transmembrane domain , signal transduction , biology , pollen , kinase , resolution (logic) , chemistry , microbiology and biotechnology , receptor , crystallography , biochemistry , botany , gene , artificial intelligence , pollination , computer science , mutant
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 C 2, with unit‐cell parameters a = 136.53, b = 56.01, c = 62.93 Å, β = 108.99° and two molecules per asymmetric unit.