Crystallization of L-aspartate oxidase, the first enzyme in the bacterial de novo biosynthesis of NAD

L Bacchella; C Lina; F Todone; A Negri; G Tedeschi; S Ronchi; A Mattevi

doi:10.1107/s0907444998011913

Crystallization of L-aspartate oxidase, the first enzyme in the bacterial de novo biosynthesis of NAD

Acta Crystallogr D Biol Crystallogr. 1999 Feb;55(Pt 2):549-51. doi: 10.1107/s0907444998011913.

Authors

L Bacchella¹, C Lina, F Todone, A Negri, G Tedeschi, S Ronchi, A Mattevi

Affiliation

¹ Dipartimento di Genetica e Microbiologia, Università di Pavia, Via Abbiategrasso 207, 27100 Pavia, Italy.

PMID: 10089375
DOI: 10.1107/s0907444998011913

Abstract

The flavoenzyme L-aspartate oxidase from Escherichia coli was crystallized using the hanging-drop vapour-diffusion technique with PEG 4000 as precipitant. The crystals belong to space group P3121 (or P3221) with unit-cell parameters a = b = 84.9, c = 159.9 A. A solvent content of 42% corresponds to a monomer (60 kDa) in the asymmetric unit. A complete 2.8 A resolution data set was collected using a rotating-anode X-ray generator.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Oxidoreductases / chemistry*
Crystallization
Crystallography, X-Ray
Escherichia coli / enzymology
Escherichia coli Proteins
NAD / biosynthesis*

Substances

Escherichia coli Proteins
NAD
Amino Acid Oxidoreductases
L-aspartate oxidase, E coli