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Article ; Online: Femtosecond quantification of void evolution during rapid material failure.

Coakley, James / Higginbotham, Andrew / McGonegle, David / Ilavsky, Jan / Swinburne, Thomas D / Wark, Justin S / Rahman, Khandaker M / Vorontsov, Vassili A / Dye, David / Lane, Thomas J / Boutet, Sébastien / Koglin, Jason / Robinson, Joseph / Milathianaki, Despina

Science advances

2020 Volume 6, Issue 51

Abstract: Understanding high-velocity impact, and the subsequent high strain rate material deformation and potential catastrophic failure, is of critical importance across a range of scientific and engineering disciplines that include astrophysics, materials ... ...

Abstract	Understanding high-velocity impact, and the subsequent high strain rate material deformation and potential catastrophic failure, is of critical importance across a range of scientific and engineering disciplines that include astrophysics, materials science, and aerospace engineering. The deformation and failure mechanisms are not thoroughly understood, given the challenges of experimentally quantifying material evolution at extremely short time scales. Here, copper foils are rapidly strained via picosecond laser ablation and probed in situ with femtosecond x-ray free electron (XFEL) pulses. Small-angle x-ray scattering (SAXS) monitors the void distribution evolution, while wide-angle scattering (WAXS) simultaneously determines the strain evolution. The ability to quantifiably characterize the nanoscale during high strain rate failure with ultrafast SAXS, complementing WAXS, represents a broadening in the range of science that can be performed with XFEL. It is shown that ultimate failure occurs via void nucleation, growth, and coalescence, and the data agree well with molecular dynamics simulations.
Language	English
Publishing date	2020-12-16
Publishing country	United States
Document type	Journal Article
ZDB-ID	2810933-8
ISSN	2375-2548 ; 2375-2548
ISSN (online)	2375-2548
ISSN	2375-2548
DOI	10.1126/sciadv.abb4434
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Book ; Online: Simulations of x-ray diffraction from uniaxially-compressed highly-textured polycrystalline targets

McGonegle, David / Milathianaki, Despina / Remington, Bruce A. / Wark, Justin S. / Higginbotham, Andrew

2015

Abstract: A growing number of shock compression experiments, especially those involving laser compression, are taking advantage of in situ x-ray diffraction as a tool to interrogate structure and microstructure evolution. Although these experiments are becoming ... ...

Abstract	A growing number of shock compression experiments, especially those involving laser compression, are taking advantage of in situ x-ray diffraction as a tool to interrogate structure and microstructure evolution. Although these experiments are becoming increasingly sophisticated, there has been little work on exploiting the textured nature of polycrystalline targets to gain information on sample response. Here, we describe how to generate simulated x-ray diffraction patterns from materials with an arbitrary texture function subject to a general deformation gradient. We will present simulations of Debye-Scherrer x-ray diffraction from highly textured polycrystalline targets that have been subjected to uniaxial compression, as may occur under planar shock conditions. In particular, we study samples with a fibre texture, and find that the azimuthal dependence of the diffraction patterns contains information that, in principle, affords discrimination between a number of similar shock-deformation mechanisms. For certain cases we compare our method with results obtained by taking the Fourier Transform of the atomic positions calculated by classical molecular dynamics simulations. Illustrative results are presented for the shock-induced $\alpha$-$\epsilon$ phase transition in iron, the $\alpha$-$\omega$ transition in titanium and deformation due to twinning in tantalum that is initially preferentially textured along [001] and [011]. The simulations are relevant to experiments that can now be performed using 4th generation light sources, where single-shot x-ray diffraction patterns from crystals compressed via laser-ablation can be obtained on timescales shorter than a phonon period. Comment: 10 pages, 4 figures; typo corrected in Fig. 1 caption
Keywords	Condensed Matter - Materials Science
Subject code	612
Publishing date	2015-01-22
Publishing country	us
Document type	Book ; Online
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Article ; Online: Optical laser systems at the Linac Coherent Light Source.

Minitti, Michael P / Robinson, Joseph S / Coffee, Ryan N / Edstrom, Steve / Gilevich, Sasha / Glownia, James M / Granados, Eduardo / Hering, Philippe / Hoffmann, Matthias C / Miahnahri, Alan / Milathianaki, Despina / Polzin, Wayne / Ratner, Daniel / Tavella, Franz / Vetter, Sharon / Welch, Marc / White, William E / Fry, Alan R

Journal of synchrotron radiation

2015 Volume 22, Issue 3, Page(s) 526–531

Abstract: Ultrafast optical lasers play an essential role in exploiting the unique capabilities of recently commissioned X-ray free-electron laser facilities such as the Linac Coherent Light Source (LCLS). Pump-probe experimental techniques reveal ultrafast ... ...

Abstract	Ultrafast optical lasers play an essential role in exploiting the unique capabilities of recently commissioned X-ray free-electron laser facilities such as the Linac Coherent Light Source (LCLS). Pump-probe experimental techniques reveal ultrafast dynamics in atomic and molecular processes and reveal new insights in chemistry, biology, material science and high-energy-density physics. This manuscript describes the laser systems and experimental methods that enable cutting-edge optical laser/X-ray pump-probe experiments to be performed at LCLS.
MeSH term(s)	California ; Crystallography, X-Ray/instrumentation ; Energy Transfer ; Equipment Design ; Equipment Failure Analysis ; Lasers ; Lighting/instrumentation ; Particle Accelerators/instrumentation ; Spectrometry, X-Ray Emission/instrumentation ; X-Rays
Language	English
Publishing date	2015-04-22
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	2021413-3
ISSN	1600-5775 ; 0909-0495
ISSN (online)	1600-5775
ISSN	0909-0495
DOI	10.1107/S1600577515006244
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Article ; Online: Ultrafast structural changes within a photosynthetic reaction centre.

Dods, Robert / Båth, Petra / Morozov, Dmitry / Gagnér, Viktor Ahlberg / Arnlund, David / Luk, Hoi Ling / Kübel, Joachim / Maj, Michał / Vallejos, Adams / Wickstrand, Cecilia / Bosman, Robert / Beyerlein, Kenneth R / Nelson, Garrett / Liang, Mengning / Milathianaki, Despina / Robinson, Joseph / Harimoorthy, Rajiv / Berntsen, Peter / Malmerberg, Erik /

Nature

2020 Volume 589, Issue 7841, Page(s) 310–314

Abstract: Photosynthetic reaction centres harvest the energy content of sunlight by transporting electrons across an energy-transducing biological membrane. Here we use time-resolved serial femtosecond ... ...

Abstract	Photosynthetic reaction centres harvest the energy content of sunlight by transporting electrons across an energy-transducing biological membrane. Here we use time-resolved serial femtosecond crystallography
MeSH term(s)	Bacteriochlorophylls/metabolism ; Binding Sites/drug effects ; Chlorophyll/metabolism ; Chlorophyll/radiation effects ; Crystallography ; Cytoplasm/metabolism ; Electron Transport/drug effects ; Electrons ; Hyphomicrobiaceae/enzymology ; Hyphomicrobiaceae/metabolism ; Lasers ; Models, Molecular ; Oxidation-Reduction/radiation effects ; Pheophytins/metabolism ; Photosynthetic Reaction Center Complex Proteins/chemistry ; Photosynthetic Reaction Center Complex Proteins/metabolism ; Photosynthetic Reaction Center Complex Proteins/radiation effects ; Protons ; Ubiquinone/analogs & derivatives ; Ubiquinone/metabolism ; Vitamin K 2/metabolism
Chemical Substances	Bacteriochlorophylls ; Pheophytins ; Photosynthetic Reaction Center Complex Proteins ; Protons ; Vitamin K 2 (11032-49-8) ; Ubiquinone (1339-63-5) ; Chlorophyll (1406-65-1) ; bacteriopheophytin (17453-58-6) ; ubiquinol (M9NL0C577Y)
Language	English
Publishing date	2020-12-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-020-3000-7
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Article ; Online: The Coherent X-ray Imaging instrument at the Linac Coherent Light Source.

Journal of synchrotron radiation

2015 Volume 22, Issue 3, Page(s) 514–519

Abstract: The Coherent X-ray Imaging (CXI) instrument specializes in hard X-ray, in-vacuum, high power density experiments in all areas of science. Two main sample chambers, one containing a 100 nm focus and one a 1 µm focus, are available, each with multiple ... ...

Abstract	The Coherent X-ray Imaging (CXI) instrument specializes in hard X-ray, in-vacuum, high power density experiments in all areas of science. Two main sample chambers, one containing a 100 nm focus and one a 1 µm focus, are available, each with multiple diagnostics, sample injection, pump-probe and detector capabilities. The flexibility of CXI has enabled it to host a diverse range of experiments, from biological to extreme matter.
MeSH term(s)	California ; Crystallography, X-Ray/instrumentation ; Energy Transfer ; Equipment Design ; Equipment Failure Analysis ; Lasers ; Lighting/instrumentation ; Molecular Imaging/instrumentation ; Particle Accelerators/instrumentation ; Spectrometry, X-Ray Emission/instrumentation ; X-Rays
Language	English
Publishing date	2015-04-15
Publishing country	United States
Document type	Journal Article
ZDB-ID	2021413-3
ISSN	1600-5775 ; 0909-0495
ISSN (online)	1600-5775
ISSN	0909-0495
DOI	10.1107/S160057751500449X
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Article ; Online: The Matter in Extreme Conditions instrument at the Linac Coherent Light Source.

Nagler, Bob / Arnold, Brice / Bouchard, Gary / Boyce, Richard F / Boyce, Richard M / Callen, Alice / Campell, Marc / Curiel, Ruben / Galtier, Eric / Garofoli, Justin / Granados, Eduardo / Hastings, Jerry / Hays, Greg / Heimann, Philip / Lee, Richard W / Milathianaki, Despina / Plummer, Lori / Schropp, Andreas / Wallace, Alex /

Welch, Marc / White, William / Xing, Zhou / Yin, Jing / Young, James / Zastrau, Ulf / Lee, Hae Ja

Journal of synchrotron radiation

2015 Volume 22, Issue 3, Page(s) 520–525

Abstract: The LCLS beam provides revolutionary capabilities for studying the transient behavior of matter in extreme conditions. The particular strength of the Matter in Extreme Conditions instrument is that it combines the unique LCLS beam with high-power optical ...

Abstract	The LCLS beam provides revolutionary capabilities for studying the transient behavior of matter in extreme conditions. The particular strength of the Matter in Extreme Conditions instrument is that it combines the unique LCLS beam with high-power optical laser beams, and a suite of dedicated diagnostics tailored for this field of science. In this paper an overview of the beamline, the capabilities of the instrumentation, and selected highlights of experiments and commissioning results are presented.
Language	English
Publishing date	2015-04-21
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2021413-3
ISSN	1600-5775 ; 0909-0495
ISSN (online)	1600-5775
ISSN	0909-0495
DOI	10.1107/S1600577515004865
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Article ; Online: Direct observation of ultrafast collective motions in CO myoglobin upon ligand dissociation.

Barends, Thomas R M / Foucar, Lutz / Ardevol, Albert / Nass, Karol / Aquila, Andrew / Botha, Sabine / Doak, R Bruce / Falahati, Konstantin / Hartmann, Elisabeth / Hilpert, Mario / Heinz, Marcel / Hoffmann, Matthias C / Köfinger, Jürgen / Koglin, Jason E / Kovacsova, Gabriela / Liang, Mengning / Milathianaki, Despina / Lemke, Henrik T / Reinstein, Jochen /

Roome, Christopher M / Shoeman, Robert L / Williams, Garth J / Burghardt, Irene / Hummer, Gerhard / Boutet, Sébastien / Schlichting, Ilme

Science (New York, N.Y.)

2015 Volume 350, Issue 6259, Page(s) 445–450

Abstract: The hemoprotein myoglobin is a model system for the study of protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon ...

Abstract	The hemoprotein myoglobin is a model system for the study of protein dynamics. We used time-resolved serial femtosecond crystallography at an x-ray free-electron laser to resolve the ultrafast structural changes in the carbonmonoxy myoglobin complex upon photolysis of the Fe-CO bond. Structural changes appear throughout the protein within 500 femtoseconds, with the C, F, and H helices moving away from the heme cofactor and the E and A helices moving toward it. These collective movements are predicted by hybrid quantum mechanics/molecular mechanics simulations. Together with the observed oscillations of residues contacting the heme, our calculations support the prediction that an immediate collective response of the protein occurs upon ligand dissociation, as a result of heme vibrational modes coupling to global modes of the protein.
MeSH term(s)	Animals ; Carbon Monoxide/chemistry ; Crystallography, X-Ray ; Heme/chemistry ; Horses ; Iron/chemistry ; Ligands ; Molecular Dynamics Simulation ; Motion ; Myoglobin/chemistry ; Photolysis ; Protein Structure, Secondary
Chemical Substances	Ligands ; Myoglobin ; carboxymyoglobin ; Heme (42VZT0U6YR) ; Carbon Monoxide (7U1EE4V452) ; Iron (E1UOL152H7)
Language	English
Publishing date	2015-10-23
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.aac5492
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Article ; Online: From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography.

Dods, Robert / Båth, Petra / Arnlund, David / Beyerlein, Kenneth R / Nelson, Garrett / Liang, Mengling / Harimoorthy, Rajiv / Berntsen, Peter / Malmerberg, Erik / Johansson, Linda / Andersson, Rebecka / Bosman, Robert / Carbajo, Sergio / Claesson, Elin / Conrad, Chelsie E / Dahl, Peter / Hammarin, Greger / Hunter, Mark S / Li, Chufeng /

Lisova, Stella / Milathianaki, Despina / Robinson, Joseph / Safari, Cecilia / Sharma, Amit / Williams, Garth / Wickstrand, Cecilia / Yefanov, Oleksandr / Davidsson, Jan / DePonte, Daniel P / Barty, Anton / Brändén, Gisela / Neutze, Richard

Structure (London, England : 1993)

2017 Volume 25, Issue 9, Page(s) 1461–1468.e2

Abstract: Serial protein crystallography was developed at X-ray free-electron lasers (XFELs) and is now also being applied at storage ring facilities. Robust strategies for the growth and optimization of microcrystals are needed to advance the field. Here we ... ...

Abstract	Serial protein crystallography was developed at X-ray free-electron lasers (XFELs) and is now also being applied at storage ring facilities. Robust strategies for the growth and optimization of microcrystals are needed to advance the field. Here we illustrate a generic strategy for recovering high-density homogeneous samples of microcrystals starting from conditions known to yield large (macro) crystals of the photosynthetic reaction center of Blastochloris viridis (RC
Language	English
Publishing date	2017-09-05
Publishing country	United States
Document type	Journal Article
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2017.07.002
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Article ; Online: Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein.

Tenboer, Jason / Basu, Shibom / Zatsepin, Nadia / Pande, Kanupriya / Milathianaki, Despina / Frank, Matthias / Hunter, Mark / Boutet, Sébastien / Williams, Garth J / Koglin, Jason E / Oberthuer, Dominik / Heymann, Michael / Kupitz, Christopher / Conrad, Chelsie / Coe, Jesse / Roy-Chowdhury, Shatabdi / Weierstall, Uwe / James, Daniel / Wang, Dingjie /

Grant, Thomas / Barty, Anton / Yefanov, Oleksandr / Scales, Jennifer / Gati, Cornelius / Seuring, Carolin / Srajer, Vukica / Henning, Robert / Schwander, Peter / Fromme, Raimund / Ourmazd, Abbas / Moffat, Keith / Van Thor, Jasper J / Spence, John C H / Fromme, Petra / Chapman, Henry N / Schmidt, Marius

Science (New York, N.Y.)

2014 Volume 346, Issue 6214, Page(s) 1242–1246

Abstract: Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of biomolecules. We used microcrystals of photoactive yellow protein (a bacterial blue light photoreceptor) ...

Abstract	Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of biomolecules. We used microcrystals of photoactive yellow protein (a bacterial blue light photoreceptor) as a model system and obtained high-resolution, time-resolved difference electron density maps of excellent quality with strong features; these allowed the determination of structures of reaction intermediates to a resolution of 1.6 angstroms. Our results open the way to the study of reversible and nonreversible biological reactions on time scales as short as femtoseconds under conditions that maximize the extent of reaction initiation throughout the crystal.
MeSH term(s)	Bacterial Proteins/chemistry ; Bacterial Proteins/ultrastructure ; Crystallography, X-Ray/methods ; Photoreceptors, Microbial/chemistry ; Photoreceptors, Microbial/ultrastructure ; Protein Conformation ; Time Factors
Chemical Substances	Bacterial Proteins ; Photoreceptors, Microbial ; photoactive yellow protein, Bacteria
Language	English
Publishing date	2014-11-27
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	128410-1
ISSN	1095-9203 ; 0036-8075
ISSN (online)	1095-9203
ISSN	0036-8075
DOI	10.1126/science.1259357
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Article ; Online: Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography.

Nogly, Przemyslaw / Panneels, Valerie / Nelson, Garrett / Gati, Cornelius / Kimura, Tetsunari / Milne, Christopher / Milathianaki, Despina / Kubo, Minoru / Wu, Wenting / Conrad, Chelsie / Coe, Jesse / Bean, Richard / Zhao, Yun / Båth, Petra / Dods, Robert / Harimoorthy, Rajiv / Beyerlein, Kenneth R / Rheinberger, Jan / James, Daniel /

Nature communications

2016 Volume 7, Page(s) 12314

Abstract: Serial femtosecond crystallography (SFX) using X-ray free-electron laser sources is an emerging method with considerable potential for time-resolved pump-probe experiments. Here we present a lipidic cubic phase SFX structure of the light-driven proton ... ...

Abstract	Serial femtosecond crystallography (SFX) using X-ray free-electron laser sources is an emerging method with considerable potential for time-resolved pump-probe experiments. Here we present a lipidic cubic phase SFX structure of the light-driven proton pump bacteriorhodopsin (bR) to 2.3 Å resolution and a method to investigate protein dynamics with modest sample requirement. Time-resolved SFX (TR-SFX) with a pump-probe delay of 1 ms yields difference Fourier maps compatible with the dark to M state transition of bR. Importantly, the method is very sample efficient and reduces sample consumption to about 1 mg per collected time point. Accumulation of M intermediate within the crystal lattice is confirmed by time-resolved visible absorption spectroscopy. This study provides an important step towards characterizing the complete photocycle dynamics of retinal proteins and demonstrates the feasibility of a sample efficient viscous medium jet for TR-SFX.
MeSH term(s)	Bacteriorhodopsins/chemistry ; Crystallography, X-Ray/instrumentation ; Crystallography, X-Ray/methods ; Feasibility Studies ; Lasers ; Lipids/chemistry ; Protein Conformation ; Synchrotrons ; Time Factors ; Viscosity ; X-Ray Absorption Spectroscopy/instrumentation ; X-Ray Absorption Spectroscopy/methods
Chemical Substances	Lipids ; Bacteriorhodopsins (53026-44-1)
Language	English
Publishing date	2016-08-22
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/ncomms12314
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