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Purification, crystallization and preliminary X-ray diffraction studies of N-acetylglucosamine-phosphate mutase from Candida albicans.

Authors :
Nishitani, Yuichi
Maruyama, Daisuke
Nonaka, Tsuyoshi
Kita, Akiko
Fukami, Takaaki A.
Mio, Toshiyuki
Yamada-Okabe, Hisafumi
Yamada-Okabe, Toshiko
Miki, Kunio
Source :
Acta Crystallographica: Section F (Wiley-Blackwell). Apr2006, Vol. 62 Issue 4, p419-421. 3p. 1 Black and White Photograph, 1 Chart.
Publication Year :
2006

Abstract

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 P21, 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
62
Issue :
4
Database :
Academic Search Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
20386435
Full Text :
https://doi.org/10.1107/S1744309106010177