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 obtained by hanging-drop vapour diffusion using ammonium sulfate as precipitant. These crystals belong to space group P4(1)2(1)2 or its enantiomorph, with unit-cell parameters a = b = 57.5, c = 86.5 A, and have one molecule in the crystallographic asymmetric unit. Intensity data to 1.8 A resolution were collected from native SCP2 crystals using synchrotron radiation, were processed and scaled with an R(linear) = 4.9%.
Institut für Biochemie, Swiss Federal Institute of Technology (ETH), Universitätstrasse 16, CH-8092 Zürich, Switzerland.
T
T
Choinowski
J H
JH
Dyer
B
B
Maderegger
K H
KH
Winterhalter
H
H
Hauser
K
K
Piontek
D000818:Animals; D002352:Carrier Proteins / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D008970:Molecular Weight; D010940:Plant Proteins; D011817:Rabbits; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D013261:Sterols / Q000378:metabolism
D002352:Carrier Proteins; D010940:Plant Proteins; D011994:Recombinant Proteins; D013261:Sterols; C072087:sterol carrier proteins