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  • Title: Crystallization and preliminary X-ray analysis of Candida albicans phosphomannose isomerase.
    Author: Tolley S, Davies G, Hubbard RE, Smith DJ, Proudfoot AE, Payton MA, Cleasby A, Wonacott A, Wells TN.
    Journal: J Mol Biol; 1994 Apr 01; 237(3):349-50. PubMed ID: 8145246.
    Abstract:
    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.
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