Structural highlights
Publication Abstract from PubMed
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.
Crystallization and preliminary X-ray analysis of SDR-type pyridoxal dehydrogenase from Mesorhizobium loti.,Chu HN, Kobayashi J, Yoshikane Y, Mikami B, Yagi T Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt, 6):718-20. Epub 2010 May 29. PMID:20516609[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chu HN, Kobayashi J, Yoshikane Y, Mikami B, Yagi T. Crystallization and preliminary X-ray analysis of SDR-type pyridoxal dehydrogenase from Mesorhizobium loti. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Jun 1;66(Pt, 6):718-20. Epub 2010 May 29. PMID:20516609 doi:10.1107/S1744309110015101