Specific radiation damage can be used to solve macromolecular crystal structures.
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.
Ravelli
Raimond B G
RB
European Molecular Biology Laboratory (EMBL) Grenoble Outstation, 6 rue Jules Horowitz, B.P. 181, F38042 9, Grenoble Cedex, France. ravelli@embl-grenoble.fr
Leiros
Hanna-Kirsti Schrøder
HK
Pan
Baocheng
B
Caffrey
Martin
M
McSweeney
Sean
S
D018360:Crystallography, X-Ray / Q000379:methods*; D046911:Macromolecular Substances; D009841:Oligonucleotides / Q000737:chemistry; D011506:Proteins / Q000737:chemistry; D017356:Synchrotrons / Q000295:instrumentation
D046911:Macromolecular Substances; D009841:Oligonucleotides; D011506:Proteins