Crystallization and preliminary X-ray analysis of Candida albicans phosphomannose isomerase.
Crystals of recombinant phosphomannose isomerase from Candida albicans have been obtained in a form suitable for X-ray diffraction analysis. The enzyme plays a key role in the biosynthesis of the mannan component of the fungal cell wall. It crystallizes in monoclinic space group C2, with cell dimensions a = 124.9 A, b = 52.9 A, c = 85.9 A and beta = 127.4 degrees. The crystals diffract to Bragg spacings beyond 1.7 A, native data have been collected to 2.4 A and a search for heavy-metal derivatives is in progress. The asymmetric unit contains one molecule of the enzyme (M(r) approximately 49,000) with a Vm of 2.3 A3/Da.
Tolley
S
S
epartment of Chemistry, University of York, Heslington, U.K.
Davies
G
G
Hubbard
R E
RE
Smith
D J
DJ
Proudfoot
A E
AE
Payton
M A
MA
Cleasby
A
A
Wonacott
A
A
Wells
T N
TN
D002176:Candida albicans / Q000201:enzymology*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008359:Mannose-6-Phosphate Isomerase / Q000737:chemistry*; D011994:Recombinant Proteins / Q000737:chemistry
D011994:Recombinant Proteins; D008359:Mannose-6-Phosphate Isomerase