Open AccessPurification, crystallization and preliminary X‐ray diffraction studies of N ‐acetylglucosamine‐phosphate mutase from Candida albicans
Author(s) -
Nishitani Yuichi,
Maruyama Daisuke,
aka Tsuyoshi,
Kita Akiko,
Fukami Takaaki A.,
Mio Toshiyuki,
YamadaOkabe Hisafumi,
YamadaOkabe Toshiko,
Miki Kunio
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106010177
Subject(s) - candida albicans , crystallography , crystallization , monoclinic crystal system , phosphoglycerate mutase , resolution (logic) , x ray crystallography , mutase , chemistry , materials science , enzyme , diffraction , crystal structure , biochemistry , biology , microbiology and biotechnology , physics , optics , organic chemistry , computer science , glycolysis , artificial intelligence
N ‐acetylglucosamine‐phosphate mutase (AGM1) is an essential enzyme in the synthesis of UDP‐ N ‐acetylglucosamine (UDP‐GlcNAc) in eukaryotes and belongs to the α‐ d ‐phosphohexomutase superfamily. AGM1 from Candida albicans (CaAGM1) was purified and crystallized by the sitting‐drop vapour‐diffusion method. The crystals obtained belong to the primitive monoclinic space group P 2 1 , with unit‐cell parameters a = 60.2, b = 130.2, c = 78.0 Å, β = 106.7°. The crystals diffract X‐rays to beyond 1.8 Å resolution using synchrotron radiation.
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