Crystallization and preliminary X-ray diffraction analysis of lectin-1 from Pseudomonas aeruginosa.

Karaveg K; Liu ZJ; Tempel WDoyle RJRose JPWang BC

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Crystallization and preliminary X-ray diffraction analysis of lectin-1 from Pseudomonas aeruginosa.

机译：结晶和初步的x射线衍射分析lectin-1铜绿假单胞菌。

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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.

机译：碳水化合物的识别起着作用铜绿假单胞菌的发病机理,常见导致人类的机会性感染。carbohydrate-binding蛋白质晶体铜绿假单胞菌、凝集素PA-1现在已经获得的。I222,晶胞参数= 40.25,=72.30, c = 133.82,衍射超出1.9关于旋转阳极x射线源的决议。晶体生长条件的细节,衍射数据收集和处理报告。

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《Acta crystallographica.Section D. Biological crystallography》 |2003年第7期|1241-1242|共2页
作者
Karaveg K; Liu ZJ; Tempel WDoyle RJRose JPWang BC;
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作者单位

Department of Microbiology and Immunology, University of Louisville, Louisville, KY 40292, USA.;

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正文语种英语
中图分类化学;
关键词
carbohydrate-binding protein; Pseudomonas aeruginosa; crystalsX-raysX-ray diffraction analysisCrystallizationOpportunistic Infections;

机译：carbohydrate-binding蛋白质;假单胞菌绿脓杆菌;crystalsX-raysX-ray衍射analysisCrystallizationOpportunistic感染;

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Crystallization and preliminary X-ray diffraction analysis of lectin-1 from Pseudomonas aeruginosa.

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