Details

Autor(en) / Beteiligte

• Frank, Matthias
• Carlson, David B
• Hunter, Mark S
• Williams, Garth J
• Messerschmidt, Marc
• Zatsepin, Nadia A
• Barty, Anton
• Benner, W Henry
• Chu, Kaiqin
• Graf, Alexander T
• Hau-Riege, Stefan P
• Kirian, Richard A
• Padeste, Celestino
• Pardini, Tommaso
• Pedrini, Bill
• Segelke, Brent
• Seibert, M Marvin
• Spence, John C H
• Tsai, Ching-Ju
• Lane, Stephen M
• Li, Xiao-Dan
• Schertler, Gebhard
• Boutet, Sebastien
• Coleman, Matthew
• Evans, James E

Titel

Femtosecond X-ray diffraction from two-dimensional protein crystals

Ist Teil von

• IUCrJ, 2014-03, Vol.1 (Pt 2), p.95-100

Ort / Verlag

England: International Union of Crystallography

Erscheinungsjahr

2014

Quelle

Electronic Journals Library

Beschreibungen/Notizen

• X-ray diffraction patterns from two-dimensional (2-D) protein crystals obtained using femtosecond X-ray pulses from an X-ray free-electron laser (XFEL) are presented. To date, it has not been possible to acquire transmission X-ray diffraction patterns from individual 2-D protein crystals due to radiation damage. However, the intense and ultrafast pulses generated by an XFEL permit a new method of collecting diffraction data before the sample is destroyed. Utilizing a diffract-before-destroy approach at the Linac Coherent Light Source, Bragg diffraction was acquired to better than 8.5 Å resolution for two different 2-D protein crystal samples each less than 10 nm thick and maintained at room temperature. These proof-of-principle results show promise for structural analysis of both soluble and membrane proteins arranged as 2-D crystals without requiring cryogenic conditions or the formation of three-dimensional crystals.