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Your search keyword '"Doak, RB"' showing total 4 results
Start Over Author "Doak, RB" Journal nature methods
4 results on '"Doak, RB"'

1. Illumination guidelines for ultrafast pump-probe experiments by serial femtosecond crystallography.

Author

Grünbein ML, Stricker M, Nass Kovacs G, Kloos M, Doak RB, Shoeman RL, Reinstein J, Lecler S, Haacke S, and Schlichting I

Subjects
Electromagnetic Radiation, Lasers, Light, Scattering, Radiation, Crystallography, X-Ray methods, Photons
Abstract

Time-resolved crystallography with X-ray free-electron lasers enables structural characterization of light-induced reactions on ultrafast timescales. To be biologically and chemically relevant, such studies must be carried out in an appropriate photoexcitation regime to avoid multiphoton artifacts, a common issue in recent studies. We describe numerical and experimental approaches to determine how many photons are needed for single-photon excitation in microcrystals, taking into account losses by scattering.

Published
2020
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2. Visualizing a protein quake with time-resolved X-ray scattering at a free-electron laser.

Author

Arnlund D, Johansson LC, Wickstrand C, Barty A, Williams GJ, Malmerberg E, Davidsson J, Milathianaki D, DePonte DP, Shoeman RL, Wang D, James D, Katona G, Westenhoff S, White TA, Aquila A, Bari S, Berntsen P, Bogan M, van Driel TB, Doak RB, Kjær KS, Frank M, Fromme R, Grotjohann I, Henning R, Hunter MS, Kirian RA, Kosheleva I, Kupitz C, Liang M, Martin AV, Nielsen MM, Messerschmidt M, Seibert MM, Sjöhamn J, Stellato F, Weierstall U, Zatsepin NA, Spence JC, Fromme P, Schlichting I, Boutet S, Groenhof G, Chapman HN, and Neutze R

Subjects
Phycobiliproteins chemistry, Protein Conformation radiation effects, Radiation Dosage, Energy Transfer radiation effects, Lasers, Phycobiliproteins radiation effects, Phycobiliproteins ultrastructure, Scattering, Small Angle, X-Ray Diffraction methods
Abstract

We describe a method to measure ultrafast protein structural changes using time-resolved wide-angle X-ray scattering at an X-ray free-electron laser. We demonstrated this approach using multiphoton excitation of the Blastochloris viridis photosynthetic reaction center, observing an ultrafast global conformational change that arises within picoseconds and precedes the propagation of heat through the protein. This provides direct structural evidence for a 'protein quake': the hypothesis that proteins rapidly dissipate energy through quake-like structural motions.

Published
2014
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3. In vivo protein crystallization opens new routes in structural biology.

Author

Koopmann R, Cupelli K, Redecke L, Nass K, Deponte DP, White TA, Stellato F, Rehders D, Liang M, Andreasson J, Aquila A, Bajt S, Barthelmess M, Barty A, Bogan MJ, Bostedt C, Boutet S, Bozek JD, Caleman C, Coppola N, Davidsson J, Doak RB, Ekeberg T, Epp SW, Erk B, Fleckenstein H, Foucar L, Graafsma H, Gumprecht L, Hajdu J, Hampton CY, Hartmann A, Hartmann R, Hauser G, Hirsemann H, Holl P, Hunter MS, Kassemeyer S, Kirian RA, Lomb L, Maia FR, Kimmel N, Martin AV, Messerschmidt M, Reich C, Rolles D, Rudek B, Rudenko A, Schlichting I, Schulz J, Seibert MM, Shoeman RL, Sierra RG, Soltau H, Stern S, Strüder L, Timneanu N, Ullrich J, Wang X, Weidenspointner G, Weierstall U, Williams GJ, Wunderer CB, Fromme P, Spence JC, Stehle T, Chapman HN, Betzel C, and Duszenko M

Subjects
Protein Binding radiation effects, Protein Conformation radiation effects, Proteins radiation effects, Solubility radiation effects, X-Rays, Crystallography methods, Crystallography, X-Ray methods, Proteins chemistry, Proteins ultrastructure
Abstract

Protein crystallization in cells has been observed several times in nature. However, owing to their small size these crystals have not yet been used for X-ray crystallographic analysis. We prepared nano-sized in vivo-grown crystals of Trypanosoma brucei enzymes and applied the emerging method of free-electron laser-based serial femtosecond crystallography to record interpretable diffraction data. This combined approach will open new opportunities in structural systems biology.

Published
2012
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4. Lipidic phase membrane protein serial femtosecond crystallography.

Author

Johansson LC, Arnlund D, White TA, Katona G, Deponte DP, Weierstall U, Doak RB, Shoeman RL, Lomb L, Malmerberg E, Davidsson J, Nass K, Liang M, Andreasson J, Aquila A, Bajt S, Barthelmess M, Barty A, Bogan MJ, Bostedt C, Bozek JD, Caleman C, Coffee R, Coppola N, Ekeberg T, Epp SW, Erk B, Fleckenstein H, Foucar L, Graafsma H, Gumprecht L, Hajdu J, Hampton CY, Hartmann R, Hartmann A, Hauser G, Hirsemann H, Holl P, Hunter MS, Kassemeyer S, Kimmel N, Kirian RA, Maia FR, Marchesini S, Martin AV, Reich C, Rolles D, Rudek B, Rudenko A, Schlichting I, Schulz J, Seibert MM, Sierra RG, Soltau H, Starodub D, Stellato F, Stern S, Strüder L, Timneanu N, Ullrich J, Wahlgren WY, Wang X, Weidenspointner G, Wunderer C, Fromme P, Chapman HN, Spence JC, and Neutze R

Subjects
Protein Binding, Protein Conformation radiation effects, X-Rays, Crystallography, X-Ray methods, Lipid Bilayers chemistry, Membrane Proteins chemistry, Membrane Proteins ultrastructure
Abstract

X-ray free electron laser (X-FEL)-based serial femtosecond crystallography is an emerging method with potential to rapidly advance the challenging field of membrane protein structural biology. Here we recorded interpretable diffraction data from micrometer-sized lipidic sponge phase crystals of the Blastochloris viridis photosynthetic reaction center delivered into an X-FEL beam using a sponge phase micro-jet.

Published
2012
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