Wayne W. Chan , Steven L. Roderick , David E. Cohen
{"title":"Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data","authors":"Wayne W. Chan , Steven L. Roderick , David E. Cohen","doi":"10.1016/S0167-4838(01)00318-1","DOIUrl":null,"url":null,"abstract":"<div><p>We have expressed, purified and crystallized recombinant human phosphatidylcholine transfer protein (PC-TP) and selenomethionyl PC-TP bound to dilinoleoyl phosphatidylcholine. The biochemical properties of native and selenomethionyl PC-TP were indistinguishable, and the two proteins crystallized under similar conditions. Both native and selenomethionyl PC-TP crystallized in two distinct space groups and diffracted X-rays to 2.4 Å resolution.</p></div>","PeriodicalId":100166,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","volume":"1596 1","pages":"Pages 1-5"},"PeriodicalIF":0.0000,"publicationDate":"2002-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0167-4838(01)00318-1","citationCount":"2","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0167483801003181","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 2
Abstract
We have expressed, purified and crystallized recombinant human phosphatidylcholine transfer protein (PC-TP) and selenomethionyl PC-TP bound to dilinoleoyl phosphatidylcholine. The biochemical properties of native and selenomethionyl PC-TP were indistinguishable, and the two proteins crystallized under similar conditions. Both native and selenomethionyl PC-TP crystallized in two distinct space groups and diffracted X-rays to 2.4 Å resolution.