Crystallization and preliminary investigation of single crystals of deoxyuridine triphosphate nucleotidohydrolase from Escherichia coli.

Authors :: Cedergren-Zeppezauer ES
Larsson G
Hoffmann I
Törnroos KW
Al-Karadaghi S
Nyman PO
Source :: Proteins [Proteins] 1988; Vol. 4 (1), pp. 71-5.
Publication Year :: 1988
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.

Subjects :: Amino Acid Sequence
Crystallization
Crystallography
Microscopy, Electron
Phosphates
Protein Conformation
Succinates
Escherichia coli enzymology
Pyrophosphatases

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