UCL logo

UCL Discovery

UCL home » Library Services » Electronic resources » UCL Discovery

Purification, crystallization and preliminary X-ray diffraction analysis of a fungal saponin-detoxifying enzyme

Bamford, VA; Kolade, OO; Osbourn, AE; Hemmings, AM; (2004) Purification, crystallization and preliminary X-ray diffraction analysis of a fungal saponin-detoxifying enzyme. ACTA CRYSTALLOGR D , 60 1331 - 1333. 10.1107/S0907444904011850.

Full text not available from this repository.

Abstract

Tomatinase, an extracellular enzyme belonging to family 3 of the glycosyl hydrolases, is produced by the fungal tomato-leaf pathogen Septoria lycopersici and detoxifies the saponin alpha-tomatine. An efficient strategy for purification of the enzyme from fungal culture medium has been developed. Single crystals have been grown by vapour diffusion at 289 K from 17.5%(w/v) PEG 4K, 5%(v/v) 2-propanol and 0.1 M sodium acetate pH 4.5 as precipitant. When cryoprotected at 100 K, these crystals diffract to at least 3.0 Angstrom and belong to space group P2(1)2(1)2. Based on an estimated molecular weight of 110 kDa for the glycosylated protein and assuming two molecules in the asymmetric unit, the crystals contain approximately 46% solvent.

Type:Article
Title:Purification, crystallization and preliminary X-ray diffraction analysis of a fungal saponin-detoxifying enzyme
DOI:10.1107/S0907444904011850
Keywords:SEPTORIA-LYCOPERSICI, ALPHA-TOMATINE, RESISTANCE, HYDROLASES, GENE
UCL classification:UCL > School of BEAMS > Faculty of Engineering Science > Biochemical Engineering

Archive Staff Only: edit this record