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pubmed-article:17452791pubmed:abstractTextCrystal cryocooling is usually employed to reduce radiation damage during X-ray crystallography. Recently, a high-pressure cryocooling method has been developed which results in excellent diffraction-quality crystals without the use of penetrative cryoprotectants. Three new developments of the method are presented here: (i) Xe-He high-pressure cryocooling for Xe SAD phasing, (ii) native sulfur SAD phasing and (iii) successful cryopreservation of crystals in thick-walled capillaries without additional cryoprotectants other than the native mother liquor. These developments may be useful for structural solution of proteins without the need for selenomethionine incorporation and for high-throughput protein crystallography.lld:pubmed
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pubmed-article:17452791pubmed:authorpubmed-author:GrunerSol MSMlld:pubmed
pubmed-article:17452791pubmed:authorpubmed-author:HaoQuanQlld:pubmed
pubmed-article:17452791pubmed:authorpubmed-author:KimChae UnCUlld:pubmed
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pubmed-article:17452791pubmed:dateRevised2008-11-21lld:pubmed
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pubmed-article:17452791pubmed:year2007lld:pubmed
pubmed-article:17452791pubmed:articleTitleHigh-pressure cryocooling for capillary sample cryoprotection and diffraction phasing at long wavelengths.lld:pubmed
pubmed-article:17452791pubmed:affiliationField of Biophysics, Cornell University, Ithaca, NY 14853, USA.lld:pubmed
pubmed-article:17452791pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:17452791pubmed:publicationTypeResearch Support, U.S. Gov't, Non-P.H.S.lld:pubmed
pubmed-article:17452791pubmed:publicationTypeResearch Support, N.I.H., Extramurallld:pubmed
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