title: Lobster enolase crystallized by serendipity.
abstract: An unknown protein crystallized from a lobster muscle preparation in which arginine kinase was the majority component. It was identified as enolase by peptide sequencing and activity testing, and a SIRAS electron density map showed its three-dimensional structure to be very similar to that of yeast enolase.
authors.affiliation: Laboratoire de Biologie Structurale, UMR 9920 CNRS-Université Paris-Sud, Gif-sur-Yvette, France.
authors.forename: S
authors.initials: S
authors.lastname: Duquerroy
authors.forename: G
authors.initials: G
authors.lastname: Le Bras
authors.forename: J
authors.initials: J
authors.lastname: Janin
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001122:Arginine Kinase / Q000302:isolation & purification; D003460:Crystallization; D018360:Crystallography, X-Ray; D008969:Molecular Sequence Data; D009132:Muscles / Q000201:enzymology*; D008121:Nephropidae / Q000201:enzymology*; D010751:Phosphopyruvate Hydratase / Q000737:chemistry / Q000302:isolation & purification*; D017421:Sequence Analysis; D017386:Sequence Homology, Amino Acid
chemical_list: D001122:Arginine Kinase; D010751:Phosphopyruvate Hydratase