𝔖 Bobbio Scriptorium
✦   LIBER   ✦

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

✍ Scribed by Dr. Eilia S. Cedergren-Zeppezauer; Gunilla Larsson; Ingrid Hoffmann; Karl W. Törnoos; Salam Al-Karadaghi; Per Olof Nyman

Publisher
John Wiley and Sons
Year
1988
Tongue
English
Weight
563 KB
Volume
4
Category
Article
ISSN
0887-3585

No coin nor oath required. For personal study only.

✦ Synopsis

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.

📜 SIMILAR VOLUMES

Crystallization and preliminary x-ray an
Crystallization and preliminary x-ray analysis of Escherichia coli peptidyl-tRNA hydrolase
✍ Emmanuelle Schmitt; Michel Fromant; Pierre Plateau; Yves Mechulam; Sylvain Blanq 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 30 KB 👁 2 views

## Peptidyl-tRNA hydrolase from Escherichia coli, a monomer of 21 kDa, was overexpressed from its cloned gene pth and crystallized by using polyethylene glycol as precipitant. The crystals are orthorhombic and have unit cell parameters a 5 47.24 Å, b 5 63.59 Å, and c 5 62.57 Å. They belong to spac

Crystallization of 5-aminolaevulinic aci
Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals
✍ P.T. Erskine; J. Cooper; R. Lambert; G. Lewis; S.P. Wood; P.M. Shoolingin-Jordan 📂 Article 📅 1997 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 330 KB

## Abstract 5‐Aminolaevulinic acid dehydratase (ALAD) catalyzes the formation of porphobilinogen from two molecules of 5‐aminolaevulinic acid. Both __Escherichia coli__ and __Saccharomyces cerevisiae__ ALADs are homo‐octameric enzymes which depend on Zn^2+^ for catalytic activity and are potently i

Crystallization and preliminary X-ray an
Crystallization and preliminary X-ray analysis of the monomeric Cu, Zn superoxide dismutase from Escherichia coli
✍ Andrea Battistoni; Silvia Folcarelli; Giuseppe Rotilio; Alessandro Desideri; Cle 📂 Article 📅 1996 🏛 Cold Spring Harbor Laboratory Press 🌐 English ⚖ 315 KB

## Abstract The Cu, Zn superoxide dismutase (Cu, Zn SOD) originally isolated from the periplasmic space of __Escherichia coli__ has been cloned and overexpressed in the __E. coli__ strain BMH 71/18. The protein has been purified as a single component of 17,000 Da, corresponding to one subunit of th

Purification, crystallization, and preli
Purification, crystallization, and preliminary X-ray studies of a bifunctional 5,10-methenyl/methylene tetrahydrofolate cyclohydrolase/dehydrogenase from Escherichia coli
✍ Edwin Cheung; Linda D'Ari; Jesse C. Rabinowitz; David H. Dyer; Jie-Yu Huang; Bar 📂 Article 📅 1997 🏛 John Wiley and Sons 🌐 English ⚖ 32 KB 👁 2 views

A bifunctional enzyme that catalyzes the conversion of formyltetrahydrofolate to methylene-tetrahydrofolate (5,10methenyltetrahydrofolate cyclohydrolase and 5,10-methylene tetrahydrofolate dehydrogenase), has been subcloned from a cDNA library, purified to homogeneity, and crystallized. The crystals