Domain organization and properties of LB lysozyme crystals down to submicron size.
New topographic details appeared evident in protein crystal buffered with glycerol solution native on mica by atomic force microscopy and after laser irradiation on glass by light microscopy. This observation indicates the existence of distinct domains in the 3D crystal organisation that are quite different in size and number between the lysozyme crystals grown by Langmuir-Blodgett (LB) nanotemplate with respect to traditional hanging-drop vapour diffusion. Nanodiffraction by highly focused synchrotron radiation of laser cut submicron crystals confirmed the atomic structure of all residues of LB lysozyme crystals as being the most resistant to radiation damage. Crystals grown by LB nanotemplate still diffracted at good resolution after several steps of X-ray 'burning', while the classical crystals decayed very quickly at the same exposure.
Pechkova
Eugenia
E
CIRSDNNOB, University of Genoa, Corso Europa 30, 16132 Genoa, Italy.
Nicolini
Claudio
C
D000538:Aluminum Silicates / Q000737:chemistry; D002021:Buffers; D003460:Crystallization; D005990:Glycerol / Q000737:chemistry; D018625:Microscopy, Atomic Force / Q000379:methods; D018613:Microscopy, Confocal / Q000379:methods; D009113:Muramidase / Q000737:chemistry*; D053758:Nanoparticles / Q000737:chemistry*; D036103:Nanotechnology / Q000379:methods; D017434:Protein Structure, Tertiary; D017356:Synchrotrons; D014961:X-Ray Diffraction
D000538:Aluminum Silicates; D002021:Buffers; D009113:Muramidase; D005990:Glycerol; C011934:mica