Barata, L.; Sousa Silva, M.; Schuldt, L.; da Costa, G.; Tomás, A.M.; Ferreira, A.E.N.; Weiss, M.S.; Ponces Freire, A.; Cordeiro, C. : Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of glyoxalase I from Leishmania infantum. Acta Crystallographica F 66 (2010), p. 571-574
10.1107/S1744309110010754
Abstract:
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 rodshaped form. While the cube-shaped form did not diffract X-rays at all, the rod-shaped form exhibited diffraction to about 2.0 A ˚ resolution. The crystals belonged to space group P21212, with unit-cell parameters a = 130.03, b = 148.51, c = 50.63A ˚ and three dimers of the enzyme per asymmetric unit.