Chicken liver basic fatty acid-binding protein (pI = 9.0). Purification, crystallization and preliminary X-ray data.
Chicken liver basic fatty acid-binding protein (pI = 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 A and c = 138.1 A or orthorhombic, space group P2(1)2(1)2(1) with a = 60.7 A, b = 40.1 A and c = 66.7 A. The second form appears to be more suitable for X-ray diffraction studies, it diffracts to at least 2.8 A resolution and it is believed to contain one protein molecule in the crystallographic asymmetric unit.
Scapin
G
G
Department of Organic Chemistry, University of Padova, Italy.
Spadon
P
P
Pengo
L
L
Mammi
M
M
Zanotti
G
G
Monaco
H L
HL
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002352:Carrier Proteins / Q000302:isolation & purification*; D002645:Chickens; D003461:Crystallography; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D007526:Isoelectric Point; D008099:Liver / Q000032:analysis*; D008970:Molecular Weight; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins; D014961:X-Ray Diffraction
D000596:Amino Acids; D002352:Carrier Proteins; C490174:Fabp7 protein, rat; D000071438:Fatty Acid-Binding Protein 7; D050556:Fatty Acid-Binding Proteins; D009363:Neoplasm Proteins; D009419:Nerve Tissue Proteins