Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of glyoxalase I from Leishmania infantum

• Type: Article in International Scientific Journal
• Date: 2010

Authors

barata, l (Author) Other; silva, ms (Author) Other; schuldt, l (Author) Other; da costa, g (Author) Other; tomas, am (Author) FCUP; ferreira, aen (Author) Other; weiss, ms (Author) Other; freire, ap (Author) Other; cordeiro, c (Author) Other

Journal

Title: Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Vol. 66

Pages: 571-574

ISSN: 1744-3091

Publisher: John Wiley & Sons

Indexing

ISI Web of Knowledge - 6 Citations

Scopus - 6 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-003-6SS

DOI: 10.1107/S1744309110010754

Abstract (EN): Glyoxalase I (GLO1) is the first of the two glyoxalase-pathway enzymes. It catalyzes the formation of S-D-lactoyltrypanothione from the non-enzymatically formed hemithioacetal of methylglyoxal and reduced trypanothione. In order to understand its substrate binding and catalytic mechanism, GLO1 from Leishmania infantum was cloned, overexpressed in Escherichia coli, purified and crystallized. Two crystal forms were obtained: a cube-shaped form and a rod-shaped form. While the cube-shaped form did not diffract X-rays at all, the rod-shaped form exhibited diffraction to about 2.0 angstrom resolution. The crystals belonged to space group P21212, with unit-cell parameters a = 130.03, b = 148.51, c = 50.63 angstrom and three dimers of the enzyme per asymmetric unit.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 4