Comparison of lysozyme structures derived from thin-film-based and classical crystals

Acta Crystallogr D Biol Crystallogr. 2005 Jun;61(Pt 6):803-8. doi: 10.1107/S0907444905006578. Epub 2005 May 26.

Abstract

The present report is dedicated to a systematic comparison of crystal structures produced by the nanobiofilm template method and by the classical hanging-drop vapour-diffusion method. Crystals grown by the innovative nanostructured template method appear indeed radiation-resistant even in the presence of a third-generation highly focused beam at the European Synchrotron Radiation Facility. The implications of this finding for protein crystallography are discussed here in terms of water redistribution and of the detailed atomic resolution comparative studies of the two crystal structures with or without nanobiofilm template, as emerging also from circular-dichroism and thermal denaturation studies.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Chickens
  • Crystallization / methods
  • Crystallography, X-Ray / methods*
  • Muramidase / chemistry*
  • Nanotechnology / methods*
  • Protein Structure, Tertiary

Substances

  • Muramidase