Crystallization, data collection and phasing of two digestive lysozymes from Musca domestica

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Aug 1;62(Pt 8):750-2. doi: 10.1107/S1744309106024201. Epub 2006 Jul 24.

Abstract

Lysozymes are mostly known for their defensive role against bacteria, but in several animals lysozymes have a digestive function. Here, the initial crystallographic characterization of two digestive lysozymes from Musca domestica are presented. The proteins were crystallized using the sitting-drop vapour-diffusion method in the presence of ammonium sulfate or PEG/2-propanol as the precipitant. X-ray diffraction data were collected to a maximum resolution of 1.9 angstroms using synchrotron radiation. The lysozyme 1 and 2 crystals belong to the monoclinic space group P2(1) (unit-cell parameters a = 36.52, b = 79.44, c = 45.20 angstroms, beta = 102.97 degrees) and the orthorhombic space group P2(1)2(1)2 (unit-cell parameters a = 73.90, b = 96.40, c = 33.27 angstroms), respectively. The crystal structures were solved by molecular replacement and structure refinement is in progress.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Crystallization
  • Digestive System / enzymology
  • Houseflies / enzymology*
  • Isoenzymes / chemistry
  • Isoenzymes / isolation & purification
  • Muramidase / chemistry*
  • Muramidase / isolation & purification
  • Synchrotrons
  • X-Ray Diffraction

Substances

  • Isoenzymes
  • Muramidase