Linked Life Data

10531514

Source:http://linkedlifedata.com/resource/pubmed/id/10531514

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 10
pubmed:dateCreated
1999-11-23
pubmed:abstractText
A review of the requirements for collecting X-ray diffraction data from protein crystals is given, with an emphasis on the properties of the crystal and its diffraction pattern. The size, unit-cell dimensions and perfection of the crystals can all be related to the required size and divergence of the incident X-ray beam, together with the size and spatial resolution of the detector. The X-ray beam causes primary radiation damage, even in frozen crystals. If the incident beam is very intense, temperature rises and gradients could occur in the crystal. The extent to which these problems can be overcome is also discussed.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
55
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1663-8
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Matching X-ray source, optics and detectors to protein crystallography requirements.
pubmed:affiliation
CCLRC Daresbury Laboratory, Daresbury Warrington WA4 4AD, England. c.nave@dl.ac.uk
pubmed:publicationType
Journal Article