Crystallization and Preliminary X-ray Diffraction Studies of Aes Acetyl-Esterase From Escherichia Coli

Acta Crystallogr D Biol Crystallogr. 2003 Oct;59(Pt 10):1846-8. doi: 10.1107/s0907444903017864. Epub 2003 Sep 19.

Abstract

The acetyl-esterase Aes from Escherichia coli, which belongs to the HSL group of the esterase/lipase superfamily, has been crystallized by the hanging-drop vapour-diffusion method using polyethylene glycol 8000 as a precipitant and magnesium chloride as an additive. Crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 110.0, b = 190.6, c = 218.6 A. A complete data set has been collected to 2.5 A resolution at the Elettra synchrotron source, Trieste using a single frozen crystal. Packing density considerations agree with 10-16 monomers in the asymmetric unit, with a corresponding solvent content of 61-38%.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylesterase / biosynthesis
  • Acetylesterase / chemistry*
  • Acetylesterase / genetics
  • Crystallization / methods
  • Crystallography, X-Ray / methods
  • Escherichia coli / enzymology*
  • Escherichia coli Proteins
  • Protein Conformation
  • Proteins / chemistry*
  • Proteins / metabolism
  • Recombinant Proteins / biosynthesis
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Synchrotrons

Substances

  • Escherichia coli Proteins
  • Proteins
  • Recombinant Proteins
  • AES protein, E coli
  • Acetylesterase