2oqn: Difference between revisions
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==Overview== | ==Overview== | ||
Crystal cryocooling is usually employed to reduce radiation damage during | Crystal 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thaumatococcus daniellii]] | [[Category: Thaumatococcus daniellii]] | ||
[[Category: Gruner, S | [[Category: Gruner, S M.]] | ||
[[Category: Hao, Q.]] | [[Category: Hao, Q.]] | ||
[[Category: Kim, C | [[Category: Kim, C U.]] | ||
[[Category: TAR]] | [[Category: TAR]] | ||
[[Category: capillary cryoprotection]] | [[Category: capillary cryoprotection]] | ||
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[[Category: sulfur sad phasing]] | [[Category: sulfur sad phasing]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:29 2008'' | ||
Revision as of 19:21, 21 February 2008
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High Pressure Cryocooling of Capillary Sample Cryoprotection and Diffraction Phasing at Long Wavelengths
OverviewOverview
Crystal 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.
About this StructureAbout this Structure
2OQN is a Single protein structure of sequence from Thaumatococcus daniellii with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
High-pressure cryocooling for capillary sample cryoprotection and diffraction phasing at long wavelengths., Kim CU, Hao Q, Gruner SM, Acta Crystallogr D Biol Crystallogr. 2007 May;63(Pt 5):653-9. Epub 2007, Apr 21. PMID:17452791
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