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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2008 Feb 1;64(Pt 2):88-90. doi: 10.1107/S1744309107068522. Epub 2008 Jan 18.

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 A resolution at 100 K. Crystals belong to the monoclinic space group P2(1), with unit-cell parameters a = 86.4, b = 216.6, c = 205.4 A, beta = 98.1 degrees. Molecular replacement was performed and led to the identification of six dimers per asymmetric unit.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Aldehyde Dehydrogenase / chemistry*
  • Aldehyde Dehydrogenase / isolation & purification
  • Aldehyde Dehydrogenase / metabolism
  • Base Sequence
  • Blotting, Western
  • Cloning, Molecular
  • Crystallization
  • Crystallography, X-Ray
  • DNA Primers
  • Electrophoresis, Polyacrylamide Gel
  • Pisum sativum / enzymology*
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization

Substances

  • DNA Primers
  • Recombinant Proteins
  • Aldehyde Dehydrogenase