Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius).
The crystal and molecular structure of the minor component of pike parvalbumins has been determined at 1.93 A resolution by molecular replacement (1 A = 0.1 nm). The crystals are orthorhombic, space group P2(1)2(1)2 with a = 59.62 A, b = 59.83 A and c = 26.35 A. A location of the secondary cation binding site is proposed for this parvalbumin of the beta phylogenetic series.
Declercq
J P
JP
Laboratoire de Chimie physique et de Cristallographie, Université de Louvain, Belgium.
Tinant
B
B
Parello
J
J
Etienne
G
G
Huber
R
R
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003461:Crystallography; D009124:Muscle Proteins; D010320:Parvalbumins; D012487:Salmonidae
D009124:Muscle Proteins; D010320:Parvalbumins