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Comparative Study
. 2002 Apr 1;1596(1):1-5.
doi: 10.1016/s0167-4838(01)00318-1.

Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data

Wayne W Chan  1 , Steven L Roderick, David E Cohen
Affiliations
Comparative Study

Human phosphatidylcholine transfer protein: purification, crystallization and preliminary X-ray diffraction data

Wayne W Chan et al. Biochim Biophys Acta. .

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 A resolution.

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