scholarly journals Serial Femtosecond Crystallography user's consortium apparatus at European XFEL

2014 ◽  
Vol 70 (a1) ◽  
pp. C1748-C1748
Author(s):  
Marc Messerschmidt ◽  
Leonard Chavas ◽  
Sunil Ananthaneni ◽  
Hamidreza Dadgostar ◽  
Heinz Graafsma ◽  
...  
Keyword(s):  
Protein Crystal ◽  
Pixel Detector ◽  
Single Particles ◽  
Time Resolved ◽  
X Ray ◽  
Overall Design ◽  
Laser Facility ◽  
Common Problems ◽  
Automated Procedures ◽  
Serial Femtosecond Crystallography

The Serial Femtosecond Crystallography (SFX) user's consortium apparatus is to be installed within the Single Particles, Clusters and Biomolecules (SPB) instrument of the European X-ray Free-Electron Laser facility (XFEL.EU) [1, 2]. The XFEL.EU will provide ultra-short, highly intense, coherent X-ray pulses at an unprecedented repetition rate. The experimental setup and methodological approaches of many scientific areas will be transformed, including structural biology that could potentially overcome common problems and bottlenecks encountered in crystallography, such as creating large crystals, dealing with radiation damage, or understanding sub-picosecond time-resolved phenomena. The key concept of the SFX method is based on the kinetic insertion of protein crystal samples in solution via a gas dynamic virtual nozzle jet and recording diffraction signals of individual, randomly oriented crystals passing through the XFEL beam, as first demonstrated by Chapman et al. [3]. The SFX-apparatus will refocus the beam spent by the SPB instrument into a second interaction region, in some cases enabling two parallel experiments. The planned photon energy range at the SPB instrument is from 3 to 16 keV. The Adaptive Gain Integrating Pixel Detector (AGIPD) is to be implemented in the SPB instrument, including a 4 Megapixel version for the SFX-apparatus. The AGIPD is designed to store over 350 data frames from successive pulses, and aims to collect more than 3,000 images per second. Together with the implementation of automated procedures for sample exchange and injection, high-throughput nanocrystallography experiments can be integrated at the SFX-apparatus. In this work, we review the overall design of the SFX-apparatus and discuss the main parameters and challenges

scholarly journals Segmented flow generator for serial crystallography at the European X-ray free electron laser

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Austin Echelmeier ◽  
Jorvani Cruz Villarreal ◽  
Marc Messerschmidt ◽  
Daihyun Kim ◽  
Jesse D. Coe ◽  
...  
Keyword(s):  
Free Electron ◽  
Structural Features ◽  
Protein Crystal ◽  
Liquid Sample ◽  
Time Resolved ◽  
X Ray ◽  
Flow Generator ◽  
Serial Crystallography ◽  
Serial Femtosecond Crystallography

Abstract Serial femtosecond crystallography (SFX) with X-ray free electron lasers (XFELs) allows structure determination of membrane proteins and time-resolved crystallography. Common liquid sample delivery continuously jets the protein crystal suspension into the path of the XFEL, wasting a vast amount of sample due to the pulsed nature of all current XFEL sources. The European XFEL (EuXFEL) delivers femtosecond (fs) X-ray pulses in trains spaced 100 ms apart whereas pulses within trains are currently separated by 889 ns. Therefore, continuous sample delivery via fast jets wastes >99% of sample. Here, we introduce a microfluidic device delivering crystal laden droplets segmented with an immiscible oil reducing sample waste and demonstrate droplet injection at the EuXFEL compatible with high pressure liquid delivery of an SFX experiment. While achieving ~60% reduction in sample waste, we determine the structure of the enzyme 3-deoxy-D-manno-octulosonate-8-phosphate synthase from microcrystals delivered in droplets revealing distinct structural features not previously reported.

scholarly journals The Single Particles, Clusters and Biomolecules and Serial Femtosecond Crystallography instrument of the European XFEL: initial installation

2019 ◽  
Vol 26 (3) ◽  
pp. 660-676 ◽  
Author(s):  
Adrian P. Mancuso ◽  
Andrew Aquila ◽  
Lewis Batchelor ◽  
Richard J. Bean ◽  
Johan Bielecki ◽  
...  
Keyword(s):  
Structure Determination ◽  
High Repetition Rate ◽  
Optical Systems ◽  
Diagnostic Tools ◽  
Imaging Method ◽  
Single Particles ◽  
X Ray ◽  
Data Rates ◽  
Serial Crystallography ◽  
Serial Femtosecond Crystallography

The European X-ray Free-Electron Laser (FEL) became the first operational high-repetition-rate hard X-ray FEL with first lasing in May 2017. Biological structure determination has already benefitted from the unique properties and capabilities of X-ray FELs, predominantly through the development and application of serial crystallography. The possibility of now performing such experiments at data rates more than an order of magnitude greater than previous X-ray FELs enables not only a higher rate of discovery but also new classes of experiments previously not feasible at lower data rates. One example is time-resolved experiments requiring a higher number of time steps for interpretation, or structure determination from samples with low hit rates in conventional X-ray FEL serial crystallography. Following first lasing at the European XFEL, initial commissioning and operation occurred at two scientific instruments, one of which is the Single Particles, Clusters and Biomolecules and Serial Femtosecond Crystallography (SPB/SFX) instrument. This instrument provides a photon energy range, focal spot sizes and diagnostic tools necessary for structure determination of biological specimens. The instrumentation explicitly addresses serial crystallography and the developing single particle imaging method as well as other forward-scattering and diffraction techniques. This paper describes the major science cases of SPB/SFX and its initial instrumentation – in particular its optical systems, available sample delivery methods, 2D detectors, supporting optical laser systems and key diagnostic components. The present capabilities of the instrument will be reviewed and a brief outlook of its future capabilities is also described.

scholarly journals The time-resolved hard X-ray diffraction endstation KMC-3 XPP at BESSY II

2021 ◽  
Vol 28 (3) ◽  
Author(s):  
Matthias Rössle ◽  
Wolfram Leitenberger ◽  
Matthias Reinhardt ◽  
Azize Koç ◽  
Jan Pudell ◽  
...  
Keyword(s):  
Storage Ring ◽  
Single Photon ◽  
Laser System ◽  
High Vacuum ◽  
Laser Pulses ◽  
Pixel Detector ◽  
X Ray Diffraction ◽  
Optical Pump ◽  
Time Resolved ◽  
X Ray

The time-resolved hard X-ray diffraction endstation KMC-3 XPP for optical pump/X-ray probe experiments at the electron storage ring BESSY II is dedicated to investigating the structural response of thin film samples and heterostructures after their excitation with ultrashort laser pulses and/or electric field pulses. It enables experiments with access to symmetric and asymmetric Bragg reflections via a four-circle diffractometer and it is possible to keep the sample in high vacuum and vary the sample temperature between ∼15 K and 350 K. The femtosecond laser system permanently installed at the beamline allows for optical excitation of the sample at 1028 nm. A non-linear optical setup enables the sample excitation also at 514 nm and 343 nm. A time-resolution of 17 ps is achieved with the `low-α' operation mode of the storage ring and an electronic variation of the delay between optical pump and hard X-ray probe pulse conveniently accesses picosecond to microsecond timescales. Direct time-resolved detection of the diffracted hard X-ray synchrotron pulses use a gated area pixel detector or a fast point detector in single photon counting mode. The range of experiments that are reliably conducted at the endstation and that detect structural dynamics of samples excited by laser pulses or electric fields are presented.

Time-Resolved Serial Femtosecond Crystallography at the European X-ray Free Electron Laser

2019 ◽  
Author(s):  
Marius Schmidt ◽  
Suraj Pandey ◽  
Adrian Mancuso ◽  
Richard Bean
Keyword(s):  
Free Electron ◽  
Free Electron Laser ◽  
Crystallographic Data ◽  
Time Resolved ◽  
X Ray ◽  
Serial Femtosecond Crystallography

Abstract This protocol introduces step by step into the collection of time resolved crystallographic data and their analysis at the European Free Electron Laser.

scholarly journals Coherent convergent-beam time-resolved X-ray diffraction

2014 ◽  
Vol 369 (1647) ◽  
pp. 20130325 ◽  
Author(s):  
John C. H. Spence ◽  
Nadia A. Zatsepin ◽  
Chufeng Li
Keyword(s):  
Single Shot ◽  
Beam Diameter ◽  
X Ray Diffraction ◽  
Single Particles ◽  
Time Resolved ◽  
X Ray ◽  
Challenges And Opportunities ◽  
Phase Sensitive ◽  
Diffraction Patterns ◽  
Convergent Beam

The use of coherent X-ray lasers for structural biology allows the use of nanometre diameter X-ray beams with large beam divergence. Their application to the structure analysis of protein nanocrystals and single particles raises new challenges and opportunities. We discuss the form of these coherent convergent-beam (CCB) hard X-ray diffraction patterns and their potential use for time-resolved crystallography, normally achieved by Laue (polychromatic) diffraction, for which the monochromatic laser radiation of a free-electron X-ray laser is unsuitable. We discuss the possibility of obtaining single-shot, angle-integrated rocking curves from CCB patterns, and the dependence of the resulting patterns on the focused beam coordinate when the beam diameter is larger or smaller than a nanocrystal, or smaller than one unit cell. We show how structure factor phase information is provided at overlapping interfering orders and how a common phase origin between different shots may be obtained. Their use in refinement of the phase-sensitive intensity between overlapping orders is suggested.

scholarly journals Two mirror X-ray pulse split and delay instrument for femtosecond time resolved investigations at the LCLS free electron laser facility

2016 ◽  
Vol 24 (11) ◽  
pp. 11768 ◽  
Author(s):  
Nora Berrah ◽  
Li Fang ◽  
Brendan F Murphy ◽  
Edwin Kukk ◽  
Timur Y. Osipov ◽  
...  
Keyword(s):  
Free Electron ◽  
Free Electron Laser ◽  
Time Resolved ◽  
X Ray ◽  
Laser Facility

Protein crystal dynamics studied by time-resolved analysis of X-ray diffuse scattering

Nature ◽  
1989 ◽  
Vol 338 (6217) ◽  
pp. 665-666 ◽  
Author(s):  
G. U. Nienhaus ◽  
J. Heinzl ◽  
E. Huenges ◽  
F. Parak
Keyword(s):  
Diffuse Scattering ◽  
Protein Crystal ◽  
Time Resolved ◽  
X Ray ◽  
Crystal Dynamics

Some topical issues in research on short-pulse laser-produced plasmas

1980 ◽  
Vol 298 (1439) ◽  
pp. 351-364 ◽  
Keyword(s):  
Recent Work ◽  
Pulse Laser ◽  
Short Pulse ◽  
Fast Time ◽  
Physical Processes ◽  
Time Resolved ◽  
X Ray ◽  
Short Pulse Laser ◽  
Laser Facility ◽  
Interaction Phenomena

A brief review is presented of the main physical processes in laser-produced plasmas. This is followed by illustrations taken from recent work at the S.R.C. Central Laser Facility of the use of X-ray and visible streak cameras for fast time resolved measurements of implosion and interaction phenomena in laser-produced plasmas.

scholarly journals Measurements of the ablation-front trajectory and low-mode nonuniformity in direct-drive implosions using x-ray self-emission shadowgraphy

2015 ◽  
Vol 3 ◽  
Author(s):  
D.T. Michel ◽  
A.K. Davis ◽  
W. Armstrong ◽  
R. Bahr ◽  
R. Epstein ◽  
...  
Keyword(s):  
Plasma Phys ◽  
X Rays ◽  
Direct Drive ◽  
Time Resolved ◽  
X Ray ◽  
Laser Facility ◽  
Omega Laser ◽  
Control Fusion ◽  
Pm 10 ◽  
Ablation Front

Self-emission x-ray shadowgraphy provides a method to measure the ablation-front trajectory and low-mode nonuniformity of a target imploded by directly illuminating a fusion capsule with laser beams. The technique uses time-resolved images of soft x-rays ( ${>}1$  keV) emitted from the coronal plasma of the target imaged onto an x-ray framing camera to determine the position of the ablation front. Methods used to accurately measure the ablation-front radius ( ${\it\delta}R=\pm 1.15~{\rm\mu}\text{m}$ ), image-to-image timing ( ${\it\delta}({\rm\Delta}t)=\pm 2.5$  ps) and absolute timing ( ${\it\delta}t=\pm 10$  ps) are presented. Angular averaging of the images provides an average radius measurement of ${\it\delta}(R_{\text{av}})=\pm 0.15~{\rm\mu}\text{m}$ and an error in velocity of ${\it\delta}V/V=\pm 3\%$ . This technique was applied on the Omega Laser Facility [Boehly et al., Opt. Commun. 133, 495 (1997)] and the National Ignition Facility [Campbell and Hogan, Plasma Phys. Control. Fusion 41, B39 (1999)].

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