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Expression, crystallization and preliminary X-ray data analysis of NT-ALS9, a fungal adhesin from Candida albicans

DOI: 10.1107/S1744309111003460 DOI Help
PMID: 21505243 PMID Help

Authors: Paula Salgado (Imperial College London) , Robert Yan (Imperial College London) , Fiona Rowan (Imperial College London) , Ernesto Cota-segura (Imperial College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology And Crystallization Communications

State: Published (Approved)
Published: April 2011
Diamond Proposal Number(s): 1227

Abstract: Candida albicans is a common human fungal commensal that can also cause a range of infections from skin/mucosal `thrush' to severe systemic candidiasis. Adherence to host cells is one of the key determinants of Candida pathogenesis. The Als family of surface proteins has been implicated in adhesion of C. albicans, yet limited information has been published on the structure and mechanism of these fungal adhesins. The N-terminal region of these proteins has been shown to possess adhesive properties, making it a possible target for new therapeutic strategies. Recombinant NT-Als9-2 from C. albicans (residues 18-329) was overexpressed in Escherichia coli, purified and crystallized. Diffraction data were collected to 2.0 Å resolution. The crystals belonged to space group P212121, with unit-cell parameters a = 34.73, b = 68.71, c = 120.03 Å, [alpha] = [beta] = [gamma] = 90° and one molecule in the asymmetric unit. Platinum-derivatized crystals belonged to the same space group, with similar unit-cell parameters, although they were not completely isomorphous.

Journal Keywords: Candida Albicans; Adhesion; Fungal Pathogenicity; Adhesins; Als9-2.

Subject Areas: Medicine, Biology and Bio-materials

Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-Macromolecular Crystallography