+ Site Statistics
+ Search Articles
+ PDF Full Text Service
How our service works
Request PDF Full Text
+ Follow Us
Follow on Facebook
Follow on Twitter
Follow on LinkedIn
+ Subscribe to Site Feeds
Most Shared
PDF Full Text
+ Translate
+ Recently Requested

Specific radiation damage can be used to solve macromolecular crystal structures



Specific radiation damage can be used to solve macromolecular crystal structures



Structure 11(2): 217-224



The use of third generation synchrotron sources has led to renewed concern about the effect of ionizing radiation on crystalline biological samples. In general, the problem is seen as one to be avoided. However, in this paper, it is shown that, far from being a hindrance to successful structure determination, radiation damage provides an opportunity for phasing macromolecular structures. This is successfully demonstrated for both a protein and an oligonucleotide, by way of which complete models were built automatically. The possibility that, through the exploitation of radiation damage, the phase problem could become less of a barrier to macromolecular crystal structure determination is discussed.

Please choose payment method:






(PDF emailed within 0-6 h: $19.90)

Accession: 011385369

Download citation: RISBibTeXText

PMID: 12575941

DOI: 10.1016/s0969-2126(03)00006-6


Related references

RABDAM : quantifying specific radiation damage in individual protein crystal structures. Journal of Applied Crystallography 51(Pt 2): 552-559, 2018

Using X-ray absorption spectra to monitor specific radiation damage to anomalously scattering atoms in macromolecular crystallography. Acta Crystallographica. Section D Biological Crystallography 63(Pt 7): 759-768, 2007

Effects of crystal twinning on the ability to solve a macromolecular structure using multiwavelength anomalous diffraction. Acta Crystallographica Section D Biological Crystallography 56(8): 959-964, 2000

Combining X-ray and electron-microscopy data to solve crystal structures. Acta Crystallographica. Section D Biological Crystallography 64(Pt 1): 70-75, 2008

Publication of macromolecular crystal structures. Febs Letters 380(3): 301, 1996

REFMAC5 for the refinement of macromolecular crystal structures. Acta Crystallographica. Section D Biological Crystallography 67(Pt 4): 355-367, 2011

Does NMR mean "not for molecular replacement"? Using NMR-based search models to solve protein crystal structures. Structure 8(11): R213-R220, 2000

Using electron microscopy to complement X-ray powder diffraction data to solve complex crystal structures. Chemical Communications 2009(12): 1439-1451, 2009

Automated identification of elemental ions in macromolecular crystal structures. Acta Crystallographica. Section D Biological Crystallography 70(Pt 4): 1104-1114, 2014

Validation tools: Can they indicate the information content of macromolecular crystal structures?. Structure 6(6): 685-690, 1998

Ab initio solution of macromolecular crystal structures without direct methods. Proceedings of the National Academy of Sciences of the United States of America 114(14): 3637-3641, 2017

Diffract-and-destroy: can X-ray lasers "solve" the radiation damage problem?. Ultramicroscopy 108(12): 1502-1503, 2008

Radiation damage in macromolecular cryocrystallography. Current Opinion in Structural Biology 16(5): 624-629, 2006

Radiation Damage in Macromolecular Crystallography. Methods in Molecular Biology 1607: 467-489, 2017

AMPLE: a cluster-and-truncate approach to solve the crystal structures of small proteins using rapidly computed ab initio models. Acta Crystallographica. Section D Biological Crystallography 68(Pt 12): 1622-1631, 2012