Linked Life Data

20683008

Source:http://linkedlifedata.com/resource/pubmed/id/20683008

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2010-8-4
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1791-7530
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
30
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2745-8
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Domain organization and properties of LB lysozyme crystals down to submicron size.
pubmed:affiliation
CIRSDNNOB, University of Genoa, Corso Europa 30, 16132 Genoa, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't