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Article: Solution of protein crystallographic structures by high-pressure cryocooling and noble-gas phasing

TitleSolution of protein crystallographic structures by high-pressure cryocooling and noble-gas phasing
Authors
Issue Date2006
PublisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1
Citation
Acta Crystallographica Section D: Biological Crystallography, 2006, v. 62 n. 7, p. 687-694 How to Cite?
AbstractRoom-pressure flash-cryocooling of protein crystals is the standard way to reduce radiation damage during data collection. Typically, it is necessary to find cryoprotection conditions by trial and error, a process that is not always successful. Recently, a new method, high-pressure cryocooling, was developed that does not require penetrative cryoprotectants and typically yields very high quality diffraction. Since this method involves helium gas as a pressurizing medium, it was of great interest to see whether the method could be extended to diffraction phasing by the incorporation of heavy noble gases such as krypton. A modified Kr-He high-pressure cyrocooling procedure is described wherein crystals are first pressurized with krypton gas to 10 MPa for 1 h. The krypton pressure is then released and the crystals are repressurized with helium over 150 MPa and cooled to liquid-nitrogen temperatures. Porcine pancreas elastase (PPE; 240 residues, 26 kDa) was selected as a test case for this study. Excellent diffraction was achieved by high-pressure cryocooling without penetrating cryoprotectants. A single 0.31 occupied krypton site in a PPE molecule [Bijvoet amplitude ratio (〈|ΔF|〉/〈F〉) of 0.53%] was successfully used for SAD phasing at 1.3 Å. This method has the potential to greatly simplify obtaining protein structures. © 2006 International Union of Crystallography - all rights reserved.
Persistent Identifierhttp://hdl.handle.net/10722/91925
ISSN
2013 Impact Factor: 7.232
2015 SCImago Journal Rankings: 3.088
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChae, UKen_HK
dc.contributor.authorHao, Qen_HK
dc.contributor.authorGruner, SMen_HK
dc.date.accessioned2010-09-17T10:30:43Z-
dc.date.available2010-09-17T10:30:43Z-
dc.date.issued2006en_HK
dc.identifier.citationActa Crystallographica Section D: Biological Crystallography, 2006, v. 62 n. 7, p. 687-694en_HK
dc.identifier.issn0907-4449en_HK
dc.identifier.urihttp://hdl.handle.net/10722/91925-
dc.description.abstractRoom-pressure flash-cryocooling of protein crystals is the standard way to reduce radiation damage during data collection. Typically, it is necessary to find cryoprotection conditions by trial and error, a process that is not always successful. Recently, a new method, high-pressure cryocooling, was developed that does not require penetrative cryoprotectants and typically yields very high quality diffraction. Since this method involves helium gas as a pressurizing medium, it was of great interest to see whether the method could be extended to diffraction phasing by the incorporation of heavy noble gases such as krypton. A modified Kr-He high-pressure cyrocooling procedure is described wherein crystals are first pressurized with krypton gas to 10 MPa for 1 h. The krypton pressure is then released and the crystals are repressurized with helium over 150 MPa and cooled to liquid-nitrogen temperatures. Porcine pancreas elastase (PPE; 240 residues, 26 kDa) was selected as a test case for this study. Excellent diffraction was achieved by high-pressure cryocooling without penetrating cryoprotectants. A single 0.31 occupied krypton site in a PPE molecule [Bijvoet amplitude ratio (〈|ΔF|〉/〈F〉) of 0.53%] was successfully used for SAD phasing at 1.3 Å. This method has the potential to greatly simplify obtaining protein structures. © 2006 International Union of Crystallography - all rights reserved.en_HK
dc.languageengen_HK
dc.publisherWiley-Blackwell Publishing, Inc.. The Journal's web site is located at http://www.wiley.com/bw/editors.asp?ref=0907-4449&site=1en_HK
dc.relation.ispartofActa Crystallographica Section D: Biological Crystallographyen_HK
dc.titleSolution of protein crystallographic structures by high-pressure cryocooling and noble-gas phasingen_HK
dc.typeArticleen_HK
dc.identifier.emailHao, Q: qhao@hku.hken_HK
dc.identifier.authorityHao, Q=rp01332en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1107/S0907444906014727en_HK
dc.identifier.pmid16790924-
dc.identifier.scopuseid_2-s2.0-33745664787en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33745664787&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume62en_HK
dc.identifier.issue7en_HK
dc.identifier.spage687en_HK
dc.identifier.epage694en_HK
dc.identifier.isiWOS:000238447500001-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridChae, UK=14022481900en_HK
dc.identifier.scopusauthoridHao, Q=7102508868en_HK
dc.identifier.scopusauthoridGruner, SM=7102958350en_HK
dc.identifier.citeulike605319-

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