Abstract
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 22 12 with a = b = 60.2 Å and c = 138.1 Å or orthorhombic, space group P2 12 12 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.
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