title: Crystal structure determination and refinement of pike 4.10 parvalbumin (minor component from Esox lucius).
abstract: 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.
authors.affiliation: Laboratoire de Chimie physique et de Cristallographie, Université de Louvain, Belgium.
authors.forename: J P
authors.initials: JP
authors.lastname: Declercq
authors.forename: B
authors.initials: B
authors.lastname: Tinant
authors.forename: J
authors.initials: J
authors.lastname: Parello
authors.forename: G
authors.initials: G
authors.lastname: Etienne
authors.forename: R
authors.initials: R
authors.lastname: Huber
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003461:Crystallography; D009124:Muscle Proteins; D010320:Parvalbumins; D012487:Salmonidae
chemical_list: D009124:Muscle Proteins; D010320:Parvalbumins