The DOI matches its Crossref record; 26 of the 26 references it cites were found in a registry or an index.
Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements
Open accessAbstract
X-ray free-electron lasers have enabled new approaches to the structural determination of protein crystals that are too small or radiation-sensitive for conventional analysis1. For sufficiently short pulses, diffraction is collected before significant changes occur to the sample, and it has been predicted that pulses as short as 10 fs may be required to acquire atomic-resolution structural information1,2,3,4. Here, we describe a mechanism unique to ultrafast, ultra-intense X-ray experiments that allows structural information to be collected from crystalline samples using high radiation doses without the requirement for the pulse to terminate before the onset of sample damage. Instead, the diffracted X-rays are gated by a rapid loss of crystalline periodicity, producing apparent pulse lengths significantly shorter than the duration of the incident pulse. The shortest apparent pulse lengths occur at the highest resolution, and our measurements indicate that current X-ray free-electron laser technology5 should enable structural determination from submicrometre protein crystals with atomic resolution. Researchers describe a mechanism capable of compressing fast and intense X-ray pulses through the rapid loss of crystalline periodicity. It is hoped that this concept, combined with X-ray free-electron laser technology, will allow scientists to obtain structural information at atomic resolutions.
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Cites
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Self-citationFemtosecond X-ray protein nanocrystallography
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Self-citationSerial time-resolved crystallography of photosystem II using a femtosecond X-ray laser
Kupitz, C., Basu, S., Grotjohann, I., Fromme, R., Zatsepin, N. A., Rendek, K. N., Hunter, M. S., Shoeman, R. L., White, T. A., Wang, D., et al. (2014) · Nature · doi:10.1038/nature13453 · Cited by 477
Self-citationSerial Femtosecond Crystallography of G Protein–Coupled Receptors
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Self-citationNatively Inhibited Trypanosoma brucei Cathepsin B Structure Determined by Using an X-ray Laser
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Self-citationSimultaneous Femtosecond X-ray Spectroscopy and Diffraction of Photosystem II at Room Temperature
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Metadata
- Authors
- Barty, A., Caleman, C., Aquila, A., Timneanu, N., Lomb, L., White, T. A., Andreasson, J., Arnlund, D., Bajt, S., Barends, T. R. M., Barthelmess, M., Bogan, M. J., Bostedt, C., Bozek, J. D., Coffee, R., Coppola, N., Davidsson, J., DePonte, D. P., Doak, R. B., Ekeberg, T., Elser, V., Epp, S. W., Erk, B., Fleckenstein, H., Foucar, L., Fromme, P., Graafsma, H., Gumprecht, L., Hajdu, J., Hampton, C. Y., Hartmann, R., Hartmann, A., Hauser, G., Hirsemann, H., Holl, P., Hunter, M. S., Johansson, L., Kassemeyer, S., Kimmel, N., Kirian, R. A., Liang, M., Maia, F. R. N. C., Malmerberg, E., Marchesini, S., Martin, A. V., Nass, K., Neutze, R., Reich, C., Rolles, D., Rudek, B., Rudenko, A., Scott, H., Schlichting, I., Schulz, J., Seibert, M. M., Shoeman, R. L., Sierra, R. G., Soltau, H., Spence, J. C. H., Stellato, F., Stern, S., Strüder, L., Ullrich, J., Wang, X., Weidenspointner, G., Weierstall, U., Wunderer, C. B., & Chapman, H. N.
- Venue
- Nature Photonics
- Published
- 2011-12-18
- Volume
- 6
- Issue
- 1
- Pages
- 35-40
- ISSN
- 1749-4885 (ISSN-L)
- 1749-4893
- OpenAlex
- W2058837354
- Cited by
- 344
- References
- 26
- FWCI
- 31.63
- Type
- journal article
- Language
- en
- Open access
- green
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- Barty, A., Caleman, C., Aquila, A., Timneanu, N., Lomb, L., White, T. A., Andreasson, J., Arnlund, D., Bajt, S., Barends, T. R. M., Barthelmess, M., Bogan, M. J., Bostedt, C., Bozek, J. D., Coffee, R., Coppola, N., Davidsson, J., DePonte, D. P., Doak, R. B., . . . Chapman, H. N. (2012). Self-terminating diffraction gates femtosecond X-ray nanocrystallography measurements. Nature Photonics. https://doi.org/10.1038/nphoton.2011.297
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