TY  - JOUR
AU  - Borshchevskiy, Valentin
AU  - Round, Ekaterina
AU  - Erofeev, Ivan
AU  - Weik, Martin
AU  - Ishchenko, Andrii
AU  - Gushchin, Ivan
AU  - Mishin, Alexey
AU  - Willbold, Dieter
AU  - Büldt, Georg
AU  - Gordeliy, Valentin
TI  - Low-dose X-ray radiation induces structural alterations in proteins
JO  - Acta crystallographica / D
VL  - 70
IS  - 10
SN  - 1399-0047
CY  - Copenhagen
PB  - Munksgaard
M1  - FZJ-2015-00123
SP  - 2675 - 2685
PY  - 2014
AB  - 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.
LB  - PUB:(DE-HGF)16
UR  - <Go to ISI:>//WOS:000343060900017
C6  - pmid:25286851
DO  - DOI:10.1107/S1399004714017295
UR  - https://juser.fz-juelich.de/record/186014
ER  -