Albrecht Reinhard, Zeth Kornelius, Söding Johannes, Lupas Andrei, Linke Dirk
Max Planck Institute of Biochemistry, Department of Membrane Biochemistry, Am Klopferspitz 18, D-82152 Martinsried, Germany.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Apr 1;62(Pt 4):415-8. doi: 10.1107/S1744309106010190. Epub 2006 Mar 25.
OmpW is an eight-stranded 21 kDa molecular-weight beta-barrel protein from the outer membrane of Gram-negative bacteria. It is a major antigen in bacterial infections and has implications in antibiotic resistance and in the oxidative degradation of organic compounds. OmpW from Escherichia coli was cloned and the protein was expressed in inclusion bodies. A method for refolding and purification was developed which yields properly folded protein according to circular-dichroism measurements. The protein has been crystallized and crystals were obtained that diffracted to a resolution limit of 3.5 angstroms. The crystals belong to space group P422, with unit-cell parameters a = 122.5, c = 105.7 angstroms. A homology model of OmpW is presented based on known structures of eight-stranded beta-barrels, intended for use in molecular-replacement trials.
外膜孔蛋白W（OmpW）是一种来自革兰氏阴性菌外膜的、分子量为21 kDa的八链β桶状蛋白。它是细菌感染中的主要抗原，与抗生素耐药性以及有机化合物的氧化降解有关。克隆了来自大肠杆菌的OmpW，并使其在包涵体中表达。开发了一种重折叠和纯化方法，根据圆二色性测量结果，该方法可产生正确折叠的蛋白质。该蛋白质已被结晶，并获得了衍射分辨率极限为3.5埃的晶体。这些晶体属于空间群P422，晶胞参数a = 122.5，c = 105.7埃。基于八链β桶状蛋白的已知结构，提出了OmpW的同源模型，用于分子置换试验。
