Open AccessPurification, crystallization and preliminary X‐ray diffraction studies of UDP‐ N ‐acetylglucosamine pyrophosphorylase from Candida albicans
Author(s) -
Maruyama Daisuke,
Nishitani Yuichi,
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/s1744309106044186
Subject(s) - orthorhombic crystal system , triclinic crystal system , candida albicans , crystallization , crystallography , substrate (aquarium) , chemistry , diffraction , materials science , crystal structure , biology , optics , microbiology and biotechnology , physics , organic chemistry , ecology
UDP‐ N ‐acetylglucosamine pyrophosphorylase (UAP) is an essential enzyme in the synthesis of UDP‐ N ‐acetylglucosamine. UAP from Candida albicans was purified and crystallized by the sitting‐drop vapour‐diffusion method. The crystals of the substrate and product complexes both diffract X‐rays to beyond 2.3 Å resolution using synchrotron radiation. The crystals of the substrate complex belong to the triclinic space group P 1, with unit‐cell parameters a = 47.77, b = 62.89, c = 90.60 Å, α = 90.01, β = 97.72, γ = 92.88°, whereas those of the product complex belong to the orthorhombic space group P 2 1 2 1 2 1 , with unit‐cell parameters a = 61.95, b = 90.87, c = 94.88 Å.