Tables for
Volume F
Crystallography of biological macromolecules
Edited by M. G. Rossmann and E. Arnold

International Tables for Crystallography (2006). Vol. F, ch. 6.1, pp. 128-129   | 1 | 2 |

Section Intensity

U. W. Arndta

aLaboratory of Molecular Biology, Medical Research Council, Hills Road, Cambridge CB2 2QH, England Intensity

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The intensity of the primary X-ray beam should be such as to allow data collection in a reasonably short time; increased speed is one of the main factors which has led to the popularity of synchrotron-radiation data collection as compared to data collection using conventional sources. Moreover, the radiation damage to the sample per unit incident dose is smaller at high intensities. This does not mean that ever more intense beams are necessary for today's protein-crystallography problems; very often, the speed of data collection is limited by the read-out time of the detector; the counting-rate capabilities of present-day X-ray detectors make it impossible to use in full the intensities available at some beam lines. With the widespread use of cryocrystallographic methods (Part 10[link] ), radiation damage is no longer as severe a problem as it once was.

No doubt, the day will come when available intensities will be so high that instantaneous structure determination will become a possibility, but this will require major advances in X-ray detectors, probably in the form of the development of large pixel detectors (e.g. Beuville et al., 1997[link]).

There is still some scope for increasing the intensity of X-ray beams from conventional sources, which offer the advantage of making measurements in the local laboratory instead of at some remote central facility.


Beuville, E., Beche, J.-F., Cork, C., Douence, V., Earnest, J., Millaud, D., Nygren, H., Padmore, B., Turko, G., Zizka, G., Datte, P. & Xuong Ng, H. (1997). Two-dimensional pixel array sensor for protein crystallography. Proc. SPIE, 2859, 85–92.Google Scholar

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