Crystallization and initial X-ray analysis of rabbit mature sterol carrier protein 2

Sterol carrier protein 2 (SCP2) is a basic intracellular protein which facilitates the in vitro intermembrane transfer of cholesterol, phospholipids and glycolipids. SCP2 was expressed in Escherichia coli, purified to apparent electrophoretic homogeneity and crystallized. Single crystals were obtain...

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Bibliographic Details
Published in:Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1999-08, Vol.55 (8), p.1478-1480
Main Authors: Choinowski, Thomas, Dyer, James H., Maderegger, Bernhard, Winterhalter, Kaspar H., Hauser, Helmut, Piontek, Klaus
Format: Article
Language:English
Subjects:
Animals
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - isolation & purification
Crystallization
Crystallography, X-Ray
Escherichia coli - genetics
intramembrane transfer
Molecular Weight
Plant Proteins
Rabbits
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Recombinant Proteins - isolation & purification
sterol carrier protein
Sterols - metabolism
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Description
Summary:Sterol carrier protein 2 (SCP2) is a basic intracellular protein which facilitates the in vitro intermembrane transfer of cholesterol, phospholipids and glycolipids. SCP2 was expressed in Escherichia coli, purified to apparent electrophoretic homogeneity and crystallized. Single crystals were obtained by hanging‐drop vapour diffusion using ammonium sulfate as precipitant. These crystals belong to space group P41212 or its enantiomorph, with unit‐cell parameters a = b = 57.5, c = 86.5 Å, and have one molecule in the crystallographic asymmetric unit. Intensity data to 1.8 Å resolution were collected from native SCP2 crystals using synchrotron radiation, were processed and scaled with an Rlinear = 4.9%.
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444999007106