Acta Crystallographica Section F

Structural Biology and Crystallization Communications

Volume 64, Part 2 (February 2008)

crystallization communications

Acta Cryst. (2008). F64, 88-90 [ doi:10.1107/S1744309107068522 ]

Purification, crystallization and preliminary crystallographic study of a recombinant plant aminoaldehyde dehydrogenase from Pisum sativum

M. Tylichová, P. Briozzo, D. Kopecný, J. Ferrero, S. Moréra, N. Joly, J. Snégaroff and M. Sebela

Abstract: Aminoaldehydes are products of polyamine degradation and are known to be reactive metabolites that are toxic to living cells at high concentrations. These compounds are catabolized by aminoaldehyde dehydrogenases, which are enzymes that contain a nicotinamide adenine dinucleotide coenzyme. Aminoaldehyde dehydrogenase from Pisum sativum was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop method. A complete data set was collected to 2.8 Å resolution at 100 K. Crystals belong to the monoclinic space group P2₁, with unit-cell parameters a = 86.4, b = 216.6, c = 205.4 Å, [beta] = 98.1°. Molecular replacement was performed and led to the identification of six dimers per asymmetric unit.

Keywords: aminoaldehyde dehydrogenases; Pisum sativum.