Open AccessCrystallization and preliminary X‐ray diffraction studies of l ‐rhamnose isomerase from Pseudomonas stutzeri
Author(s) -
Yoshida Hiromi,
Wayoon Poonperm,
Takada Goro,
Izumori Ken,
Kamitori Shigehiro
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s174430910601596x
Subject(s) - pseudomonas stutzeri , crystallization , isomerase , x ray crystallography , rhamnose , chemistry , materials science , biochemistry , diffraction , bacteria , biology , organic chemistry , enzyme , physics , polysaccharide , genetics , optics
l ‐Rhamnose isomerase from Pseudomonas stutzeri ( P. stutzeri l ‐RhI) catalyzes not only the reversible isomerization of l ‐rhamnose to l ‐rhamnulose, but also isomerization between various rare aldoses and ketoses. Purified His‐tagged P. stutzeri l ‐RhI was crystallized by the hanging‐drop vapour‐diffusion method. The crystals belong to the monoclinic space group P 2 1 , with unit‐cell parameters a = 74.3, b = 104.0, c = 107.0 Å, β = 106.8°. Diffraction data have been collected to 2.0 Å resolution. The molecular weight of the purified P. stutzeri l ‐RhI with a His tag at the C‐terminus was confirmed to be 47.7 kDa by MALDI–TOF mass‐spectrometric analysis and the asymmetric unit is expected to contain four molecules.