Crystallization and Initial X-Ray Analysis of Rabbit Mature Sterol Carrier Protein 2
Document Type
Article
Publication Date
8-1-1999
Abstract
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 R(linear) = 4.9%.
DOI
10.1107/S0907444999007106
Montclair State University Digital Commons Citation
Choinowski, Thomas; Dyer, Jim; Maderegger, Bernhard; Winterhalter, Kaspar H.; Hauser, Helmut; and Piontek, Klaus, "Crystallization and Initial X-Ray Analysis of Rabbit Mature Sterol Carrier Protein 2" (1999). Department of Chemistry and Biochemistry Faculty Scholarship and Creative Works. 288.
https://digitalcommons.montclair.edu/chem-biochem-facpubs/288