Open AccessCrystallization and preliminary X‐ray analysis of 4‐pyridoxolactonase from Mesorhizobium loti
Author(s) -
Matsuda Sayoko,
Yokochi Nana,
Yoshikane Yu,
Kobayashi Jun,
Huy Chu Nhat,
Baba Seiki,
Kuramitsu Seiki,
Mikami Bunzo,
Yagi Toshiharu
Publication year - 2009
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309109028772
Subject(s) - crystallization , mesorhizobium , crystallography , physics , materials science , chemistry , organic chemistry , rhizobia , nitrogen fixation , nitrogen
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 Å resolution and belonged to the monoclinic space group C 2, with unit‐cell parameters a = 77.93, b = 38.88, c = 81.60 Å, β = 117.33°. Crystals of form II diffracted to 1.9 Å resolution and belonged to the monoclinic space group C 2, with unit‐cell parameters a = 86.24, b = 39.35, c = 82.68 Å, β = 118.02°. The calculated V M values suggested that the asymmetric unit contains one molecule in both crystal forms.