title: Preliminary crystallographic analysis of the kinase domain of SAD-1, a protein essential for presynaptic differentiation in Caenorhabditis elegans.
abstract: SAD-1 is a serine/threonine kinase which plays an important role in the regulation of both neuronal polarity and synapse formation in Caenorhabditis elegans. The kinase domain of SAD-1 from C. elegans was overexpressed in Escherichia coli BL21 (DE3) cells and purified to homogeneity using nickel-nitrilotriacetic acid metal-affinity, ion-exchange and gel-filtration chromatography. Diffraction-quality crystals were grown using the sitting-drop vapour-diffusion technique from a condition consisting of 1 M CAPSO pH 9.6, 10%(w/v) polyethylene glycol 3350. The crystals belonged to the monoclinic space group C2, with unit-cell parameters a = 205.4, b = 57.1, c = 71.7 Å, β = 106.1°. X-ray diffraction data were recorded to 3.0 Å resolution from a single crystal using synchrotron radiation.
authors.affiliation: Department of BMB, Basic Medical College, Tianjin Medical University, Tianjin 300070, People's Republic of China. xjyan@tijmu.edu.cn
authors.forename: Xiaojie
authors.initials: X
authors.lastname: Yan
authors.forename: Yuequan
authors.initials: Y
authors.lastname: Shen
mesh_terms: D000818:Animals; D017173:Caenorhabditis elegans / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D047908:Intracellular Signaling Peptides and Proteins / Q000737:chemistry*; D017346:Protein Serine-Threonine Kinases / Q000737:chemistry*
chemical_list: D047908:Intracellular Signaling Peptides and Proteins; C421165:sad-1 protein, C elegans; D017346:Protein Serine-Threonine Kinases
keywords: Caenorhabditis elegans; SAD-1; neuronal polarity; serine/threonine kinases; synapse formation
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