title: Crystallization and preliminary X-ray diffraction analysis of lectin-1 from Pseudomonas aeruginosa.
abstract: Carbohydrate recognition plays a role in the pathogenesis of Pseudomonas aeruginosa, a common cause of opportunistic infection in humans. Crystals of a carbohydrate-binding protein from P. aeruginosa, lectin PA-1, have now been obtained. The crystals belong to space group I222, with unit-cell parameters a = 40.25, b = 72.30, c = 133.82 A, and diffract to beyond 1.9 A resolution on a rotating-anode X-ray source. Details of crystal-growth conditions, diffraction data collection and processing are reported.
authors.affiliation: Department of Microbiology and Immunology, University of Louisville, Louisville, KY 40292, USA.
authors.forename: Khanita
authors.initials: K
authors.lastname: Karaveg
authors.forename: Zhi Jie
authors.initials: ZJ
authors.lastname: Liu
authors.forename: Wolfram
authors.initials: W
authors.lastname: Tempel
authors.forename: Ronald J
authors.initials: RJ
authors.lastname: Doyle
authors.forename: John P
authors.initials: JP
authors.lastname: Rose
authors.forename: Bi Cheng
authors.initials: BC
authors.lastname: Wang
mesh_terms: D003460:Crystallization / Q000379:methods; D037161:Galectins / Q000737:chemistry*; D011550:Pseudomonas aeruginosa / Q000737:chemistry*; D014961:X-Ray Diffraction / Q000379:methods
chemical_list: D037161:Galectins