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  • Title: Crystallization and preliminary X-ray analysis of SDR-type pyridoxal dehydrogenase from Mesorhizobium loti.
    Author: Chu HN, Kobayashi J, Yoshikane Y, Mikami B, Yagi T.
    Journal: Acta Crystallogr Sect F Struct Biol Cryst Commun; 2010 Jun 01; 66(Pt 6):718-20. PubMed ID: 20516609.
    Abstract:
    Pyridoxal 4-dehydrogenase from Mesorhizobium loti MAFF303099 was overexpressed in Escherichia coli. The recombinant selenomethionine-substituted enzyme was purified and crystallized by the sitting-drop vapour-diffusion method using PEG 4000 as precipitant. Crystals grew in the presence of 0.45 mM NAD(+). The crystals diffracted to 2.9 A resolution and belonged to the monoclinic space group P2(1), with unit-cell parameters a = 86.20, b = 51.11, c = 91.73 A, beta = 89.36 degrees. The calculated V(M) values suggested that the asymmetric unit contained four molecules.
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