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X‐ray studies on triclinic crystals of fatty acid binding protein
Author(s) -
Pähler Arno,
Maslowska Maria,
Parge Hans E.,
Schneider Michael,
Steifa Manfred,
Saenger Wolfram,
Keuper Hermann J.K.,
Spener Friedrich
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)80603-7
Subject(s) - triclinic crystal system , polyethylene glycol , crystallography , chemistry , molecule , resolution (logic) , crystal (programming language) , fatty acid binding protein , monomer , cytosol , x ray , crystal structure , enzyme , biochemistry , organic chemistry , physics , quantum mechanics , artificial intelligence , computer science , polymer , programming language , gene
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.