title: Comparison of lysozyme structures derived from thin-film-based and classical crystals.
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.
authors.affiliation: Fondazione Elba, Via delle Testuggini, 00100 Roma, Italy.
authors.forename: Eugenia
authors.initials: E
authors.lastname: Pechkova
authors.forename: Victor
authors.initials: V
authors.lastname: Sivozhelezov
authors.forename: Giuseppe
authors.initials: G
authors.lastname: Tropiano
authors.forename: Stefano
authors.initials: S
authors.lastname: Fiordoro
authors.forename: Claudio
authors.initials: C
authors.lastname: Nicolini
mesh_terms: D000818:Animals; D002645:Chickens; D003460:Crystallization / Q000379:methods; D018360:Crystallography, X-Ray / Q000379:methods*; D009113:Muramidase / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods*; D017434:Protein Structure, Tertiary
chemical_list: D009113:Muramidase