Purification, crystallization and preliminary X-ray diffraction studies of N-acetylglucosamine-phosphate mutase from Candida albicans.
N-acetylglucosamine-phosphate mutase (AGM1) is an essential enzyme in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc) in eukaryotes and belongs to the alpha-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 P2(1), with unit-cell parameters a = 60.2, b = 130.2, c = 78.0 angstroms, beta = 106.7 degrees. The crystals diffract X-rays to beyond 1.8 angstroms resolution using synchrotron radiation.
Nishitani
Yuichi
Y
Department of Chemistry, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Maruyama
Daisuke
D
Nonaka
Tsuyoshi
T
Kita
Akiko
A
Fukami
Takaaki A
TA
Mio
Toshiyuki
T
Yamada-Okabe
Hisafumi
H
Yamada-Okabe
Toshiko
T
Miki
Kunio
K
D002176:Candida albicans / Q000201:enzymology*; D003460:Crystallization; D017875:Phosphotransferases (Phosphomutases) / Q000737:chemistry* / Q000302:isolation & purification; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D017356:Synchrotrons; D014961:X-Ray Diffraction
D011994:Recombinant Proteins; D017875:Phosphotransferases (Phosphomutases); C018718:phosphoacetylglucosamine mutase