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2OQN

High Pressure Cryocooling of Capillary Sample Cryoprotection and Diffraction Phasing at Long Wavelengths

Summary for 2OQN
Entry DOI10.2210/pdb2oqn/pdb
DescriptorThaumatin-1, D(-)-TARTARIC ACID (3 entities in total)
Functional Keywordshigh pressure cryocooling, capillary cryoprotection, sulfur sad phasing, plant protein
Biological sourceThaumatococcus daniellii (miracle fruit)
Cellular locationCytoplasmic vesicle: P02883
Total number of polymer chains1
Total formula weight22377.15
Authors
Kim, C.U.,Hao, Q.,Gruner, S.M. (deposition date: 2007-01-31, release date: 2007-05-01, Last modification date: 2024-11-13)
Primary citationKim, C.U.,Hao, Q.,Gruner, S.M.
High-pressure cryocooling for capillary sample cryoprotection and diffraction phasing at long wavelengths.
Acta Crystallogr.,Sect.D, 63:653-659, 2007
Cited by
PubMed Abstract: 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.
PubMed: 17452791
DOI: 10.1107/S0907444907011924
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.9 Å)
Structure validation

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