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Comparison of lysozyme structures derived from thin-film-based and classical crystals
- Source :
- Acta Crystallographica Section D Biological Crystallography. 61:803-808
- Publication Year :
- 2005
- Publisher :
- International Union of Crystallography (IUCr), 2005.
-
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.
- Subjects :
- Materials science
Synchrotron radiation
Nanotechnology
General Medicine
Crystal structure
Crystallography, X-Ray
Protein Structure, Tertiary
chemistry.chemical_compound
chemistry
Structural Biology
Chemical physics
Atomic resolution
X-ray crystallography
Animals
Muramidase
Redistribution (chemistry)
Thin film
Lysozyme
Crystallization
Chickens
Template method pattern
Subjects
Details
- ISSN :
- 09074449
- Volume :
- 61
- Database :
- OpenAIRE
- Journal :
- Acta Crystallographica Section D Biological Crystallography
- Accession number :
- edsair.doi.dedup.....ddbc65862f750fc181d03f09c8254691