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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2009 Sep 1;65(Pt 9):886-9. doi: 10.1107/S1744309109028772. Epub 2009 Aug 22.

Crystallization and preliminary X-ray analysis of 4-pyridoxolactonase from Mesorhizobium loti.

Author information

1
Faculty of Agriculture, Graduate School of Integral Arts and Science, Kochi University, Monobe, Nankoku, Kochi, Japan.

Abstract

4-pyridoxolactonase from Mesorhizobium loti MAFF303099 has been overexpressed in Escherichia coli. The recombinant enzyme was purified and was crystallized by the sitting-drop vapour-diffusion method using PEG 4000 and ammonium sulfate as precipitants. Crystals of the free enzyme (form I) and of the 5-pyridoxolactone-bound enzyme (form II) grew under these conditions. Crystals of form I diffracted to 2.0 A resolution and belonged to the monoclinic space group C2, with unit-cell parameters a = 77.93, b = 38.88, c = 81.60 A, beta = 117.33 degrees. Crystals of form II diffracted to 1.9 A resolution and belonged to the monoclinic space group C2, with unit-cell parameters a = 86.24, b = 39.35, c = 82.68 A, beta = 118.02 degrees. The calculated V(M) values suggested that the asymmetric unit contains one molecule in both crystal forms.

PMID:
19724124
PMCID:
PMC2795592
DOI:
10.1107/S1744309109028772
[Indexed for MEDLINE]
Free PMC Article

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