title: Crystallization and preliminary investigation of single crystals of deoxyuridine triphosphate nucleotidohydrolase from Escherichia coli.
abstract: Deoxyuridine triphosphate nucleotidohydrolase (dUTPase), an enzyme in the nucleotide metabolism that is a pyrophosphatase hydrolyzing dUTP, has been crystallized. The crystals belong to the trigonal space group R3 and diffract beyond 2 A. The native dUTPase crystals and a mercury derivative are stable in the X-ray beam and are suitable for a high resolution X-ray structure analysis.
authors.affiliation: Department of Zoological Cell Biology, Wenner-Gren Institute, University of Stockholm, Sweden.
authors.forename: E S
authors.initials: ES
authors.lastname: Cedergren-Zeppezauer
authors.forename: G
authors.initials: G
authors.lastname: Larsson
authors.forename: I
authors.initials: I
authors.lastname: Hoffmann
authors.forename: K W
authors.initials: KW
authors.lastname: Törnroos
authors.forename: S
authors.initials: S
authors.lastname: Al-Karadaghi
authors.forename: P O
authors.initials: PO
authors.lastname: Nyman
mesh_terms: D000595:Amino Acid Sequence; D003460:Crystallization; D003461:Crystallography; D004926:Escherichia coli / Q000201:enzymology*; D008854:Microscopy, Electron; D010710:Phosphates; D011487:Protein Conformation; D011755:Pyrophosphatases; D013386:Succinates
chemical_list: D010710:Phosphates; D013386:Succinates; D011755:Pyrophosphatases; C020020:dUTP pyrophosphatase