CRYSTALLOGRAPHIC ANALYSIS OF FERRIC IRON BINDING PROTEIN BY MAD

MAD 对三价铁结合蛋白的晶体学分析

• 批准号: 6586506
• 负责人: CHRISTOPHER M BRUNS
• 金额: $ 14.32万
• 依托单位: STANFORD UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 2002
• 资助国家: 美国
• 起止时间: 2002-03-01 至 2003-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6586506
• 关键词: bacteria; bioimaging /biomedical imaging; biomaterials; biomedical resource; infection; radiography; structural biology

Multiwavelength anomalous dispersion (MAD) data using anomalous scattering from selenium and iron will be used to determine the structure of ferric iron binding protein (FBP) from Haemophilus influenzae. This protein is vital to several pathogenic bacteria and is a promising target of structure-based drug design. Attempts to determine the crystal structure by traditional methods have been extremely frustrating. Very strong anomalous scattering from the iron atom along with incorporated seleno-methionine will make this an ideal candidate for MAD phasing. The crystals diffract to 1.6 E resolution.

多波长反常色散（MAD）数据的利用