High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography
- S. Boutet, L. Lomb, I. Schlichting
- 20 July 2012
Serial femtosecond crystallography (SFX) is applied using an x-ray free-electron laser (XFEL) to obtain high-resolution structural information from microcrystals of the well-characterized model protein lysozyme, demonstrating the immediate relevance of SFX for analyzing the structure of the large group of difficult-to-crystallize molecules.
Identifying the Minimal Copper- and Zinc-binding Site Sequence in Amyloid-β Peptides*
- V. Minicozzi, F. Stellato, S. Morante
- 18 April 2008
Journal of Biological Chemistry
The atomic structure around the metal-binding site in samples where amyloid-β (Aβ) peptides are complexed with either Cu(II) or Zn(II), and the histidine residues coordinated to the metal in the various peptides studied are determined.
Room-temperature macromolecular serial crystallography using synchrotron radiation
- F. Stellato, D. Oberthür, H. Chapman
- 30 May 2014
The room-temperature structure of lysozyme is determined using 40000 individual diffraction patterns from micro-crystals flowing in liquid suspension across a synchrotron microfocus beamline.
Serial crystallography on in vivo grown microcrystals using synchrotron radiation
- C. Gati, G. Bourenkov, L. Redecke
- 10 February 2014
The structure solution of T. brucei cathepsin B from 80 in vivo grown crystals with an average volume of 9 µm3 obtained by serial synchrotron crystallography at a microfocus beamline is reported.
Serial time-resolved crystallography of photosystem II using a femtosecond X-ray laser
- Christopher Kupitz, S. Basu, P. Fromme
- 9 July 2014
Time resolved experiments on PSII nano/microcrystals from Thermosynechococcus elongatus performed with the recently developed technique of serial femtosecond crystallography provide evidence that PSII undergoes significant conformational changes at the electron acceptor side and at the Mn4CaO5 core of the OEC.
Crystallographic data processing for free-electron laser sources
- T. White, A. Barty, H. Chapman
- 15 June 2013
Materials Science, Physics
Acta Crystallographica Section D: Biological…
A processing pipeline for diffraction data acquired using the ‘serial crystallography’ methodology with a free-electron laser source is described with reference to the crystallographic analysis suite…
Time-resolved protein nanocrystallography using an X-ray free-electron laser
- A. Aquila, M. Hunter, H. Chapman
- 23 January 2012
The first time-resolved femtosecond serial X-ray crystallography results from an irreversible photo-chemical reaction at the Linac Coherent Light Source are obtained.
Natively Inhibited Trypanosoma brucei Cathepsin B Structure Determined by Using an X-ray Laser
- L. Redecke, K. Nass, H. Chapman
- 11 January 2013
The structure reveals the mechanism of native TbCatB inhibition and demonstrates that new biomolecular information can be obtained by the “diffraction-before-destruction” approach of x-ray free-electron lasers from hundreds of thousands of individual microcrystals.
Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser
- David Arnlund, L. Johansson, R. Neutze
- 10 August 2014
This work demonstrates an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein, providing direct structural evidence for a 'protein quake'.
In vivo protein crystallization opens new routes in structural biology
- R. Koopmann, K. Cupelli, M. Duszenko
- 29 January 2012
Chemistry, Materials Science
N nano-sized in vivo–grown crystals of Trypanosoma brucei enzymes are prepared and the emerging method of free-electron laser-based serial femtosecond crystallography is applied to record interpretable diffraction data to open new opportunities in structural systems biology.