Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data.
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 A resolution.
Chan
Wayne W
WW
Department of Medicine, Marion Bessin Liver Research Center, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Roderick
Steven L
SL
Cohen
David E
DE
D000727:Androgen-Binding Protein; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D003001:Cloning, Molecular; D003460:Crystallization; D004926:Escherichia coli / Q000235:genetics; D006801:Humans; D049488:Phosphatidylethanolamine Binding Protein; D049294:Phospholipid Transfer Proteins; D014961:X-Ray Diffraction
D000727:Androgen-Binding Protein; D002352:Carrier Proteins; C511482:PEBP1 protein, human; D049488:Phosphatidylethanolamine Binding Protein; D049294:Phospholipid Transfer Proteins