Home News About Us Contact Contributors Disclaimer Privacy Policy Help FAQ

Home
Search
Quick Search
Advanced
Fulltext
Browse
Collections
Persons
My eDoc
Session History
Login
Name:
Password:
Documentation
Help
Support Wiki
Direct access to
document ID:


          Institute: MPI für medizinische Forschung     Collection: Jahrbuch 2012     Display Documents



ID: 638122.0, MPI für medizinische Forschung / Jahrbuch 2012
Self−terminating diffraction gates femtosecond X−ray nanocrystallography measurements
Translation of Title:Self−terminating diffraction gates femtosecond X−ray nanocrystallography measurements
Authors:Barty, Anton; Caleman, Carl; Aquila, Andrew; Timneanu, Nicusor; Lomb, Lukas; White, Thomas A.; Andreasson, Jakob; Arnlund, David; Bajt, Saša; Barends, Thomas; Barthelmess, Miriam; Bogan, Michael J.; Bostedt, Christoph; Bozek, John D.; Coffee, Ryan N.; Coppola, Nicola; Davidsson, Jan; DePonte, Daniel P.; Doak, R. Bruce; Ekeberg, Tomas; Elser, Veit; Epp, Sascha W.; Erk, Benjamin; Fleckenstein, Holger; Foucar, Lutz; Fromme, Petra; Graafsma, Heinz; Gumprecht, Lars; Hajdu, Janos; Hampton, Christina Y.; Hartmann, Robert; Hartmann, Andreas; Hauser, Günter; Hirsemann, Helmut; Holl, Peter; Hunter, Mark S.; Johansson, Linda; Kassemeyer, Stephan; Kimmel, Nils; Kirian, Richard A.; Liang, Mengning; Maia, Filipe R. N. C.; Malmerberg, Erik; Marchesini, Stefano; Martin, Andrew V.; Nass, Karol; Neutze, Richard; Reich, Christian; Rolles, Daniel; Rudek, Benedikt; Rudenko, Artem; Scott, Howard; Schlichting, Ilme; Schulz, Joachim; Seibert, M. Marvin; Shoeman, Robert L.; Sierra, Raymond G.; Soltau, Heike; Spence, John C. H.; Stellato, Francesco; Stern, Stephan; Strüder, Lothar; Ullrich, Joachim; Wang, Xiaoyu; Weidenspointner, Georg; Weierstall, Uwe; Wunderer, Cornelia B.; Chapman, Henry N.
Language:English
Date of Publication (YYYY-MM-DD):2012-01-01
Title of Journal:Nature Photonics
Journal Abbrev.:Nature Photonics
Volume:6
Issue / Number:1
Start Page:35
End Page:40
Review Status:Peer-review
Audience:Experts Only
Intended Educational Use:No
Abstract / Description: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
External Publication Status:published
Document Type:Article
Communicated by:Wulf Kaiser
Affiliations:MPI für medizinische Forschung/Abteilung Biophysik
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Molecular chaperones
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Heme and Flavin Enzymes
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Analytical Protein Biochemistry
MPI für medizinische Forschung/Abteilung Biomolekulare Mechanismen/Coherent diffractive imaging
Identifiers:LOCALID:7766
URI:http%3A%2F%2Fwww.nature.com%2Fnphoton%2Fjournal%2F...
URI:http%3A%2F%2Fwww.nature.com%2Fnphoton%2Fjournal%2F...
URI:http%3A%2F%2Fwww.nature.com%2Fnphoton%2Fjournal%2F...
DOI:10.1038%2Fnphoton.2011.297
Full Text:
Sorry, no privileges
The scope and number of records on eDoc is subject to the collection policies defined by each institute - see "info" button in the collection browse view.