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: 6437424
• 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: 2001
• 资助国家: 美国
• 起止时间: 2001-03-01 至 2002-02-28
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/6437424
• 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.

使用反常色散的多波长反常色散 (MAD) 数据 硒和铁的散射将用于确定 嗜血杆菌三价铁结合蛋白 (FBP) 的结构 流感。 这种蛋白质对多种病原菌至关重要 是基于结构的药物设计的一个有前途的目标。 尝试 传统方法测定晶体结构 非常令人沮丧。 来自铁的非常强烈的异常散射 原子与掺入的硒代蛋氨酸将使其成为理想的 MAD 阶段的候选者。 晶体衍射分辨率为 1.6 E。