title: Crystallization and preliminary X-ray crystallographic analysis of the extracellular domain of LePRK2 from Lycopersicon esculentum.
abstract: The tomato (Lycopersicon esculentum) pollen-specific receptor kinase 2 (LePRK2) is a member of the large receptor-like kinase (RLK) family and is expressed specifically in mature pollen and pollen tubes in L. esculentum. Like other RLKs, LePRK2 contains a characteristic N-terminal leucine-rich repeat (LRR) extracellular domain, the primary function of which is in protein-protein interactions. The LePRK2 LRR is likely to bind candidate ligands from the external environment, leading to a signal transduction cascade required for successful pollination. LePRK2-LRR was purified using an insect-cell secretion expression system and was crystallized using the vapour-diffusion method. The crystals diffracted to a resolution of 2.50 Å and belonged to space group I4(1)22, with unit-cell parameters a = b = 93.94, c = 134.44 Å and one molecule 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: D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray / Q000379:methods*; D017931:DNA Primers; D018551:Solanum lycopersicum / Q000201:enzymology*; D011487:Protein Conformation; D011493:Protein Kinase C / Q000737:chemistry*
chemical_list: D017931:DNA Primers; C061570:protein kinase N; D011493:Protein Kinase C
keywords: LRR; LePRK2; Lycopersicon esculentum; receptor-like kinases