Crystallization and Preliminary X-ray Analysis of Human Plasma Apolipoprotein C-I

• Published in: Journal of molecular biology Vol. 236; no. 1; pp. 382 - 384
• Main Authors: Weisgraber, Karl H., Newhouse, Yvonne M., McPherson, Alexander
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 11.02.1994; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Apolipoprotein C-I; Apolipoproteins C - chemistry; Apolipoproteins C - isolation & purification; Biological and medical sciences; Chromatography, Gel; Chromatography, High Pressure Liquid; Chromatography, Ion Exchange; Crystalline structure; Crystallization; Crystallography, X-Ray - methods; Fundamental and applied biological sciences. Psychology; human apolipoprotein C-I; Humans; Lipoproteins, myelin; Molecular biophysics; Protein Conformation; protein crystals; protein structure; Proteins; Structure in molecular biology; X-ray; protein structure; human apolipoprotein C-I; X-ray; protein crystals; Human; Unit cell; Crystal form; Apolipoprotein CI; Crystallization; Apolipoproteins; X ray diffraction; Structural analysis
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1006/jmbi.1994.1146

Human apolipoprotein C-I, the smallest of the plasma apolipoproteins, is a component of several classes of plasma lipoproteins. Two crystalline forms of this protein, both suitable for high resolution X-ray diffraction analysis, have been obtained from mixture of 2-methyl-2,4-pentanediol, sodium acetate, and octyl-β-D-1-thioglucopyranoside at room temperature. The first form belongs to space group P2 1 with β = 106° and cell dimensions of a = 38·1 Å, b = 50·8 Å and c = 34·9 Å. The asymmetric unit appears to contain two molecules of the protein. The second form belongs to space group P 2 12 12 1, with cell dimensions of a = 34·5 Å, b = 53·1 Å, c = 71·1 Å and it also appears to contain two molecules of the protein in the asymmetric unit.