This title appears in the Scientific Report :
2014
Please use the identifier:
http://dx.doi.org/10.1107/S1399004714017295 in citations.
Low-dose X-ray radiation induces structural alterations in proteins
Low-dose X-ray radiation induces structural alterations in proteins
X-ray-radiation-induced alterations to protein structures are still a severe problem in macromolecular crystallography. One way to avoid the influence of radiation damage is to reduce the X-ray dose absorbed by the crystal during data collection. However, here it is demonstrated using the example of...
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Personal Name(s): | Borshchevskiy, Valentin |
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Round, Ekaterina / Erofeev, Ivan / Weik, Martin / Ishchenko, Andrii / Gushchin, Ivan / Mishin, Alexey / Willbold, Dieter / Büldt, Georg / Gordeliy, Valentin (Corresponding Author) | |
Contributing Institute: |
Strukturbiochemie; ICS-6 |
Published in: | Acta crystallographica / D, 70 (2014) 10, S. 2675 - 2685 |
Imprint: |
Copenhagen
Munksgaard
2014
|
PubMed ID: |
25286851 |
DOI: |
10.1107/S1399004714017295 |
Document Type: |
Journal Article |
Research Program: |
Structural Biology |
Publikationsportal JuSER |
X-ray-radiation-induced alterations to protein structures are still a severe problem in macromolecular crystallography. One way to avoid the influence of radiation damage is to reduce the X-ray dose absorbed by the crystal during data collection. However, here it is demonstrated using the example of the membrane protein bacteriorhodopsin (bR) that even a low dose of less than 0.06 MGy may induce structural alterations in proteins. This dose is about 500 times smaller than the experimental dose limit which should ideally not be exceeded per data set (i.e. 30 MGy) and 20 times smaller than previously detected specific radiation damage at the bR active site. To date, it is the lowest dose at which radiation modification of a protein structure has been described. Complementary use was made of high-resolution X-ray crystallography and online microspectrophotometry to quantitatively study low-dose X-ray-induced changes. It is shown that structural changes of the protein correlate with the spectroscopically observed formation of the so-called bR orange species. Evidence is provided for structural modifications taking place at the protein active site that should be taken into account in crystallographic studies which aim to elucidate the molecular mechanisms of bR function. |