Crystallization and preliminary investigation of single crystals of deoxyuridine triphosphate nucleotidohydrolase from Escherichia coli.
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.
Cedergren-Zeppezauer
E S
ES
Department of Zoological Cell Biology, Wenner-Gren Institute, University of Stockholm, Sweden.
Larsson
G
G
Hoffmann
I
I
Törnroos
K W
KW
Al-Karadaghi
S
S
Nyman
P O
PO
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
D010710:Phosphates; D013386:Succinates; D011755:Pyrophosphatases; C020020:dUTP pyrophosphatase