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 Å. A solvent content of 42% corresponds to a monomer (60 kDa) in the asymmetric unit. A complete 2.8 Å resolution data set was collected using a rotating-anode X-ray generator.

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. - In: ACTA CRYSTALLOGRAPHICA. SECTION D, BIOLOGICAL CRYSTALLOGRAPHY. - ISSN 0907-4449. - 55:2(1999), pp. 549-551.

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

A. Negri;G. Tedeschi;S. Ronchi;
1999

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 Å. A solvent content of 42% corresponds to a monomer (60 kDa) in the asymmetric unit. A complete 2.8 Å resolution data set was collected using a rotating-anode X-ray generator.
Settore BIO/10 - Biochimica
ACTA CRYSTALLOGRAPHICA. SECTION D, BIOLOGICAL CRYSTALLOGRAPHY
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/181338
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