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Potential for biomolecular imaging with femtosecond X-ray pulses
Computer simulations are used to investigate the structural information that can be recovered from the scattering of intense femtosecond X-ray pulses by single protein molecules and small assemblies and predict that ultrashort, high-intensity X-rays from free-electron lasers that are currently under development will provide a new approach to structural determinations with X- rays. Expand
Femtosecond X-ray protein nanocrystallography
This work offers a new approach to structure determination of macromolecules that do not yield crystals of sufficient size for studies using conventional radiation sources or are particularly sensitive to radiation damage, by using pulses briefer than the timescale of most damage processes. Expand
The catalytic pathway of horseradish peroxidase at high resolution
An effective strategy to obtain crystal structures for high-valency redox intermediates is described and a three-dimensional movie of the X-ray-driven catalytic reduction of a bound dioxygen species in horseradish peroxidase (HRP) is presented. Expand
XFEL: The European X-Ray Free-Electron Laser - Technical Design Report
Massimo Altarelli, Reinhard Brinkmann, Majed Chergui, Winfried Decking, Barry Dobson, Stefan Düsterer, Gerhard Grübel, Walter Graeff, Heinz Graafsma, Janos Hajdu, Jonathan Marangos, Joachim Pflüger,Expand
Single mimivirus particles intercepted and imaged with an X-ray laser
This work shows that high-quality diffraction data can be obtained with a single X-ray pulse from a non-crystalline biological sample, a single mimivirus particle, which was injected into the pulsed beam of a hard-X-ray free-electron laser, the Linac Coherent Light Source. Expand
Femtosecond diffractive imaging with a soft-X-ray free-electron laser
Theory predicts1,2,3,4 that, with an ultrashort and extremely bright coherent X-ray pulse, a single diffraction pattern may be recorded from a large macromolecule, a virus or a cell before the sampleExpand
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
PENICILLIN antibiotics are all produced from fermentation-derived penicillins because their chemical synthesis is not commercially viable. The key step in penicillin biosynthesis, in which both theExpand
Structure of isopenicillin N synthase complexed with substrate and the mechanism of penicillin formation.
The crystal structure of the IPNS complexed to ferrous iron and ACV bound to the active-site iron supports the hypothesis that iron-dioxygen and iron-oxo species remove the requisite hydrogens from ACV without the direct assistance of protein residues. Expand
Structure of a cephalosporin synthase
The first crystal structure of a 2-oxoacid-dependent oxygenase is reported, obtained from merohedrally twinned crystals, and a model based on these structures is proposed for ferryl formation, which is common to many mononuclear ferrous enzymes. Expand
Linac coherent light source (LCLS) conceptual design report
The Stanford Linear Accelerator Center, in collaboration with Argonne National Laboratory, Brookhaven National Laboratory, Los Alamos National Laboratory, Lawrence Livermore National Laboratory, andExpand