X-ray studies on triclinic crystals of fatty acid binding protein: Example of an extremely X-ray-resistant protein

• Published in: FEBS letters Vol. 184; no. 2; pp. 185 - 187
• Main Authors: Pähler, Arno, Maslowska, Maria, Parge, Hans E., Schneider, Michael, Steifa, Manfred, Saenger, Wolfram, Keuper, Hermann J.K., Spener, Friedrich
• Format: Journal Article
• Language: English
• Published: Amsterdam Elsevier B.V 20.05.1985; Elsevier
• Subjects: Biological and medical sciences; cattle; Crystalline structure; Crystallization Fatty acid binding protein X-ray analysis; cytosol; fatty acid-binding protein; Fundamental and applied biological sciences. Psychology; liver; Molecular biophysics; Structure in molecular biology; X-ray crystallography; Crystallization Fatty acid binding protein X-ray analysis; Binding protein; Vertebrata; Mammalia; Liver; Artiodactyla; Beef; Fatty acids; Cytosol; X ray diffraction; Ungulata; Crystalline structure
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/0014-5793(85)80603-7

Fatty acid binding protein (pI 7.0) from bovine liver cytosol was crystallized using polyethylene glycol 4000 and 6000 as precipitating agents. The crystals are triclinic, space group P1. One molecule of 14 kDa occupies the unit cell with constants a = 33.5 Å, b = 39.4 Å, c = 30.6 Å, α = 113.6°, β = 113.8°, γ = 88.8°. Crystal diffraction extends to at least 2.25 Å resolution and the crystals are stable in the X-ray beam for more than 450 h. One native data set to 2.5 Å resolution has been collected.