title: Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the LRR domain of the LePRK1 receptor-like kinase from tomato.
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.
authors.affiliation: Tsinghua-Peking Center for Life Sciences, Beijing 100084, People's Republic of China.
authors.forename: Anbi
authors.initials: A
authors.lastname: Xu
authors.affiliation: School of Life Sciences, Tsinghua University, Beijing 100084, People's Republic of China.
authors.forename: Laiqiang
authors.initials: L
authors.lastname: Huang
mesh_terms: D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray / Q000379:methods*; D018551:Solanum lycopersicum / Q000201:enzymology*; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid
chemical_list: D010940:Plant Proteins
keywords: LRR; LePRK1; Lycopersicon esculentum; receptor-like kinases