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Chicken liver basic fatty acid‐binding protein (p I = 9.0) Purification, crystallization and preliminary X‐ray data
Author(s) -
Scapin Giovanna,
Spadon Paola,
Pengo Licia,
Mammi Mario,
Zanotti Giuseppe,
Monaco Hugo L.
Publication year - 1988
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(88)80367-3
Subject(s) - orthorhombic crystal system , crystallization , tetragonal crystal system , crystallography , yield (engineering) , x ray , chemistry , resolution (logic) , homogeneous , molecule , space group , fatty acid , diffraction , x ray crystallography , crystal structure , materials science , biochemistry , organic chemistry , physics , quantum mechanics , artificial intelligence , computer science , metallurgy , thermodynamics , optics
Chicken liver basic fatty acid‐binding protein (p I = 9.0) has been purified with a high yield by a modification of a method originally applied to rat liver. The final product is highly homogeneous and can be used to grow crystals that belong to two different space groups. The crystals are either tetragonal, space group P4 2 2 1 2 with a = b = 60.2 Å and c = 138.1 Å or orthorhombic, space group P2 1 2 1 2 1 with a = 60.7 Å, b = 40.1 Å and c = 66.7 Å. The second form appears to be more suitable for X‐ray diffraction studies, it diffracts to at least 2.8 Å resolution and it is believed to contain one protein molecule in the crystallographic asymmetric unit.