2oqu
From Proteopedia
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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: Sus scrofa]] | [[Category: Sus scrofa]] | ||
- | [[Category: Gruner, S | + | [[Category: Gruner, S M.]] |
[[Category: Hao, Q.]] | [[Category: Hao, Q.]] | ||
- | [[Category: Kim, C | + | [[Category: Kim, C U.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: xenon]] | [[Category: xenon]] | ||
- | ''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 18:21:37 2008'' |
Revision as of 16:21, 21 February 2008
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High Pressure Cryocooling of Capillary Sample Cryoprotection and Diffraction Phasing at Long Wavelengths
Overview
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
2OQU is a Single protein structure of sequence from Sus scrofa with , and as ligands. Active as Pancreatic elastase, with EC number 3.4.21.36 Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 18:21:37 2008
Categories: Pancreatic elastase | Single protein | Sus scrofa | Gruner, S M. | Hao, Q. | Kim, C U. | CA | SO4 | XE | High pressure cryocooling | Sad phasing | Xenon