ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Preliminary crystallographic analysis of the kinase domain of SAD-1, a protein essential for presynaptic differentiation in Caenorhabditis elegans.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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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.
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