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• W2332380274 abstract "In this issue of Structure, Roessler et al., 2016Roessler C.G. Agarwal R. Allaire M. Alonso-Mori R. Andi B. Bachega J.F.R. Bommer M. Brewster A.S. Browne M.C. Chatterjee R. et al.Structure. 2016; 24 (this issue): 631-640Abstract Full Text Full Text PDF PubMed Scopus (78) Google Scholar present a new method to acoustically inject samples for serial femtosecond crystallography into the focus of free-electron lasers. This method can drastically reduce the sample consumption of this method. It will therefore play an important role in the mix of sample preparation technologies. In this issue of Structure, Roessler et al., 2016Roessler C.G. Agarwal R. Allaire M. Alonso-Mori R. Andi B. Bachega J.F.R. Bommer M. Brewster A.S. Browne M.C. Chatterjee R. et al.Structure. 2016; 24 (this issue): 631-640Abstract Full Text Full Text PDF PubMed Scopus (78) Google Scholar present a new method to acoustically inject samples for serial femtosecond crystallography into the focus of free-electron lasers. This method can drastically reduce the sample consumption of this method. It will therefore play an important role in the mix of sample preparation technologies. X-ray free-electron lasers (XFELs) are promising new X-ray sources for structural biology. Their potential to image single, non-crystalline biomolecules was proposed at the turn of the twenty-first century (Neutze et al., 2000Neutze R. Wouts R. van der Spoel D. Weckert E. Hajdu J. Nature. 2000; 406: 752-757Crossref PubMed Scopus (1519) Google Scholar). It took another decade to get from the proposal to first experiments, which were performed in the fall of 2009 at the Linac Coherent Light Source (LCLS) at the SLAC National Accelerator Laboratory in Menlo Park, California (Chapman et al., 2011Chapman H.N. Fromme P. Barty A. White T.A. Kirian R.A. Aquila A. Hunter M.S. Schulz J. DePonte D.P. Weierstall U. et al.Nature. 2011; 470: 73-77Crossref PubMed Scopus (1588) Google Scholar, Seibert et al., 2011Seibert M.M. Ekeberg T. Maia F.R. Svenda M. Andreasson J. Jönsson O. Odić D. Iwan B. Rocker A. Westphal D. et al.Nature. 2011; 470: 78-81Crossref PubMed Scopus (752) Google Scholar). Today, a second XFEL, the SPring-8 Angstrom Compact free electron Laser (SACLA), is operational in Japan and three more sources are under construction in South Korea and Europe. Both the European FEL in Schenefeld close to Hamburg (Germany) and the SwissFEL in Villgen (Switzerland) are expected to produce first X-rays in 2017. FELs are based on kilometer-long linear electron accelerators that produce highly brilliant short electron bunches. These electron bunches are converted into X-ray photons in alternate magnet structures, the undulators. The non-linear interaction between electrons and the increasingly strong X-ray field in an undulator produces X-ray bunches with laser-like properties. The main advantages of XFELs with respect to conventional synchrotron sources are the high peak brilliance in extremely short femtosecond pulses and the high spatial coherence. In protein crystallography, the use of high-power ultra-short pulses enables the image-before-destruction approach. The diffraction signal of a sample can be recorded in a single shot before radiation damage has time to develop. In the few tens of femtoseconds of the X-ray pulse, atoms do not move from their initial positions, which further improves the quality of acquired diffraction data. At the moment, single particle imaging is limited to rather large objects such as viruses and cell organelles. Taking the method to the next level and making it applicable to obtaining direct images from proteins or protein complexes requires further development and optimization of all the steps in the process, from sample preparation to delivery, to minimize impurities and background signals and to develop low noise and high dynamic range detectors and further advancement of phase retrieval and sorting algorithms. Serial femtosecond crystallography (SFX), on the other hand, is already proving to be a valuable technique to use with XFELs. In SFX, hundreds of thousands of single-crystal diffraction images are taken in series. Each image stems from a randomly oriented crystal. For every image, the crystal orientation is determined and the visible Bragg peaks are indexed. In this way, a complete 3D diffraction signal can be recorded and phased to a complete reconstruction of the protein structure. The SFX method depends on obtaining images from single crystals. To make the best use of the beamtime at an XFEL source, a new sample has to be delivered for each X-ray pulse. Fast detectors have to be able to record images in the repetition rate of the XFEL. Finally, fast data processing is necessary to quickly collect, pre-process, and store the high data rate. In all of these fields—sample delivery, X-ray detectors, and data handling and management—new technology is currently under development. Sample delivery for SFX is mainly based on using a liquid jet. Crystals are prepared in suspension and pressed through the focus of the XFEL in jets. With the typical, widely used gas dynamic virtual nozzles, sample speed is in the order of 20 m/s. This is fast enough to provide a new sample for each X-ray pulse at the LCLS repetition rate of 120 Hz. For the envisioned maximum repetition rate of 4.5 MHz in bunch trains of the European XFEL, faster jets are under development. A high fraction of X-ray pulses hitting a crystal can be reached by choosing an appropriate sample concentration in the suspension. From the sample point of view, however, the method is highly inefficient. In the off-time between pulses, the vast majority of crystals pass through the focus without any chance of being measured. Work by Roessler et al., 2016Roessler C.G. Agarwal R. Allaire M. Alonso-Mori R. Andi B. Bachega J.F.R. Bommer M. Brewster A.S. Browne M.C. Chatterjee R. et al.Structure. 2016; 24 (this issue): 631-640Abstract Full Text Full Text PDF PubMed Scopus (78) Google Scholar opens exciting new perspectives and provides an interesting advancement toward achieving higher sample efficiency. The authors present acoustic injectors for drop-on-demand SFX. By employing acoustic levitation, it is possible to inject single drops into the focus of the XFEL synchronized with the pulse structure. The approach to deliver one and only one protein crystal to each X-ray pulse could result in efficient use of both sample and X-rays. In practice, it is of cause not that perfect. The authors reached crystal hits in up to 34% of the X-ray pulses, a rate that is comparable to liquid jets. The real breakthrough of the new work is in sample efficiency, as Roessler et al., 2016Roessler C.G. Agarwal R. Allaire M. Alonso-Mori R. Andi B. Bachega J.F.R. Bommer M. Brewster A.S. Browne M.C. Chatterjee R. et al.Structure. 2016; 24 (this issue): 631-640Abstract Full Text Full Text PDF PubMed Scopus (78) Google Scholar show that up to 80% of the crystals in solution could be used. This far exceeds the performance of conventional jets, where only a small fraction of the crystals, typically one in two thousands, are actually measured. The method is therefore the method of choice for scarce and difficult-to-obtain samples. A clear drawback is that acoustic injectors only work in air, while many SFX experiments are today performed in vacuum to keep background scattering low. Vacuum is especially important when smaller crystals or even non-crystalline samples are to be imaged because weak scattering targets need low background environments. The future of XFELs is promising to be very exciting, as the results we have seen so far (Barends et al., 2015Barends T.R. Foucar L. Ardevol A. Nass K. Aquila A. Botha S. Doak R.B. Falahati K. Hartmann E. Hilpert M. et al.Science. 2015; 350: 445-450Crossref PubMed Scopus (289) Google Scholar, Kang et al., 2015Kang Y. Zhou X.E. Gao X. He Y. Liu W. Ishchenko A. Barty A. White T.A. Yefanov O. Han G.W. et al.Nature. 2015; 523: 561-567Crossref PubMed Scopus (580) Google Scholar, Redecke et al., 2013Redecke L. Nass K. DePonte D.P. White T.A. Rehders D. Barty A. Stellato F. Liang M. Barends T.R. Boutet S. et al.Science. 2013; 339: 227-230Crossref PubMed Scopus (356) Google Scholar, van der Schot et al., 2015van der Schot G. Svenda M. Maia F.R. Hantke M. DePonte D.P. Seibert M.M. Aquila A. Schulz J. Kirian R. Liang M. et al.Nat. Commun. 2015; 6: 5704Crossref PubMed Scopus (129) Google Scholar) are an impressive array of high quality structural information obtained on difficult systems that escaped crystallization efforts and structural characterization in the past. What is also undisputable is that we will likely depend on application of a diverse set of sample preparation techniques to ensure the high quality of XFEL performance. Therefore, we can expect to see further development of acoustic injectors, as they seem likely to play an important contribution to the mix of sample delivery methods compatible with XFELs. Acoustic Injectors for Drop-On-Demand Serial Femtosecond CrystallographyRoessler et al.StructureMarch 17, 2016In BriefAcoustic droplet ejection provides an automated tool for efficient use of protein crystals in SFX experiments. Roessler et al. used this method to deliver crystal-containing droplets into the XFEL beam to coincide with each X-ray pulse. Full-Text PDF Open Archive" @default.
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• W2332380274 title "Acoustic Injectors Meet X-Ray Free-Electron Lasers" @default.
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