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14 results on '"Arnlund, D"'

1. Conformational activation of visual rhodopsin in native disc membranes

Author

Malmerberg, E., Bovee-Geurts, P.H.M., Katona, G., Deupi, X., Arnlund, D., Wickstrand, C., Johansson, L.C., Westenhoff, S., Nazarenko, E., GF, X.S., Menzel, A., Grip, W.J. de, Neutze, R., Malmerberg, E., Bovee-Geurts, P.H.M., Katona, G., Deupi, X., Arnlund, D., Wickstrand, C., Johansson, L.C., Westenhoff, S., Nazarenko, E., GF, X.S., Menzel, A., Grip, W.J. de, and Neutze, R.

Abstract

Contains fulltext : 154870.pdf (publisher's version ) (Closed access), Rhodopsin is the G protein-coupled receptor (GPCR) that serves as a dim-light receptor for vision in vertebrates. We probed light-induced conformational changes in rhodopsin in its native membrane environment at room temperature using time-resolved wide-angle x-ray scattering. We observed a rapid conformational transition that is consistent with an outward tilt of the cytoplasmic portion of transmembrane helix 6 concomitant with an inward movement of the cytoplasmic portion of transmembrane helix 5. These movements were considerably larger than those reported from the basis of crystal structures of activated rhodopsin, implying that light activation of rhodopsin involves a more extended conformational change than was previously suggested.

Published
2015

2. Native inhibition of Trypanosoma brucei cathepsin B revealed by an X-ray laser at 2.1 \u01fa resolution

Author

Redecke L, Nass K, DePonte DP, White TA, Rehders D, Barty A, Stellato F, Liang M, Barends TRM, Boutet S, Williams GJ, Messerschmidt M, Seibert MM, Aquila A, Arnlund D, Bajt S, Barth T, Bogan MJ, Caleman C, Chao T, Doak RB, Fleckenstein H, Frank M, Fromme R, Galli L, Grotjohann I, Hunter MS, Johansson LC, Kassemeyer S, Katona G, Kirian R, Koopmann R, Kupitz C, Lomb L, Martin AV, Mogk S, Neutze R, Shoeman RL, Steinbrener J, Timneanu N, Wang D, Weierstall U, Zatsepin NA, Spence JCH, Fromme P, and Schlichting I

Published
2013

3. Time-resolved protein nanocrystallography using an X-ray free-electron laser

Author

Aquila, A, Hunter, MS, Doak, RB, Kirian, RA, Fromme, P, White, TA, Andreasson, J, Arnlund, D, Bajt, S, Barends, TRM, Barthelmess, M, Bogan, MJ, Bostedt, C, Bottin, H, Bozek, JD, Caleman, C, Coppola, N, Davidsson, J, DePonte, DP, Elser, V, Epp, SW, Erk, B, Fleckenstein, H, Foucar, L, Frank, M, Fromme, R, Graafsma, H, Grotjohann, I, Gumprecht, L, Hajdu, J, Hampton, CY, Hartmann, A, Hartmann, R, Hauriege, S, Hauser, G, Hirsemann, H, Holl, P, Holton, JM, Homke, A, and Johansso

Published
2012

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, MN, 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, and Kassem

Published
2012

5. High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography

Author

Boutet S, Lomb L, Williams GJ, Barends TRM, Aquila A, Doak RB, Weierstall U, DePonte DP, Steinbrener J, Shoeman RL, Messerschmidt M, Barty A, White TA, Kassemeyer S, Kirian RA, Seibert MM, Montanez PA, Kenney C, Herbst R, Hart P, Pines J, Haller G, Gruner SM, Philipp HT, Tate MW, Hromalik M, Koerner LJ, van Bakel N, Morse J, Ghonsalves W, Arnlund D, Bogan MJ, Caleman C, Fromme R, Hampton CY, Hunter MS, Johansson LC, Katona G, Kupitz C, Liang MN, Martin AV, Nass K, Redecke L, Stellato F, Timneanu N, and Wang DJ

Published
2012

6. Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography

Author

Johansson, LC, Arnlund, D, Katona, G, White, TA, Barty, A, DePonte, DP, Shoeman, RL, Wickstrand, C, Sharma, A, Williams, GJ, Aquila, A, Bogan, MJ, Caleman, C, Davidsson, J, Doak, RB, Frank, M, Fromme, R, Galli, L, Grotjohann, I, Hunter, MS, Kassemeyer, S, Kirian, RA, Kupitz, C, Liang, M, Lomb, L, Malmerberg, E, Martin, AV, Messerschmidt, M, Nass, K, Redecke, L, Seibert, MM, Sjoehamn, J, Steinbrener, J, Stellato, F, Wang, D, Wahlgren, WY, Weierstall, U, Westenhoff, S, Zatsepin, NA, Boutet, S, Spence, JCH, Schlichting, I, Chapman, HN, Fromme, P, Neutze, R, Johansson, LC, Arnlund, D, Katona, G, White, TA, Barty, A, DePonte, DP, Shoeman, RL, Wickstrand, C, Sharma, A, Williams, GJ, Aquila, A, Bogan, MJ, Caleman, C, Davidsson, J, Doak, RB, Frank, M, Fromme, R, Galli, L, Grotjohann, I, Hunter, MS, Kassemeyer, S, Kirian, RA, Kupitz, C, Liang, M, Lomb, L, Malmerberg, E, Martin, AV, Messerschmidt, M, Nass, K, Redecke, L, Seibert, MM, Sjoehamn, J, Steinbrener, J, Stellato, F, Wang, D, Wahlgren, WY, Weierstall, U, Westenhoff, S, Zatsepin, NA, Boutet, S, Spence, JCH, Schlichting, I, Chapman, HN, Fromme, P, and Neutze, R

Abstract

Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 Å resolution and determine its serial femtosecond crystallography structure to 3.5 Å resolution. Although every microcrystal is exposed to a dose of 33 MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.

Published
2013

10. Ultrafast structural changes within a photosynthetic reaction centre.

Author

Dods R, Båth P, Morozov D, Gagnér VA, Arnlund D, Luk HL, Kübel J, Maj M, Vallejos A, Wickstrand C, Bosman R, Beyerlein KR, Nelson G, Liang M, Milathianaki D, Robinson J, Harimoorthy R, Berntsen P, Malmerberg E, Johansson L, Andersson R, Carbajo S, Claesson E, Conrad CE, Dahl P, Hammarin G, Hunter MS, Li C, Lisova S, Royant A, Safari C, Sharma A, Williams GJ, Yefanov O, Westenhoff S, Davidsson J, DePonte DP, Boutet S, Barty A, Katona G, Groenhof G, Brändén G, and Neutze R

Subjects
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 radiation effects, Protons, Ubiquinone analogs & derivatives, Ubiquinone metabolism, Vitamin K 2 metabolism, Photosynthetic Reaction Center Complex Proteins chemistry, Photosynthetic Reaction Center Complex Proteins metabolism
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 1 using an X-ray free-electron laser 2 to observe light-induced structural changes in the photosynthetic reaction centre of Blastochloris viridis on a timescale of picoseconds. Structural perturbations first occur at the special pair of chlorophyll molecules of the photosynthetic reaction centre that are photo-oxidized by light. Electron transfer to the menaquinone acceptor on the opposite side of the membrane induces a movement of this cofactor together with lower amplitude protein rearrangements. These observations reveal how proteins use conformational dynamics to stabilize the charge-separation steps of electron-transfer reactions.

Published
2021
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11. Author Correction: Coherent diffractive imaging of microtubules using an X-ray laser.

Author

Brändén G, Hammarin G, Harimoorthy R, Johansson A, Arnlund D, Malmerberg E, Barty A, Tångefjord S, Berntsen P, DePonte DP, Seuring C, White TA, Stellato F, Bean R, Beyerlein KR, Chavas LMG, Fleckenstein H, Gati C, Ghoshdastider U, Gumprecht L, Oberthür D, Popp D, Seibert M, Tilp T, Messerschmidt M, Williams GJ, Loh ND, Chapman HN, Zwart P, Liang M, Boutet S, Robinson RC, and Neutze R

Abstract

An amendment to this paper has been published and can be accessed via a link at the top of the paper.

Published
2019
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12. Coherent diffractive imaging of microtubules using an X-ray laser.

Author

Brändén G, Hammarin G, Harimoorthy R, Johansson A, Arnlund D, Malmerberg E, Barty A, Tångefjord S, Berntsen P, DePonte DP, Seuring C, White TA, Stellato F, Bean R, Beyerlein KR, Chavas LMG, Fleckenstein H, Gati C, Ghoshdastider U, Gumprecht L, Oberthür D, Popp D, Seibert M, Tilp T, Messerschmidt M, Williams GJ, Loh ND, Chapman HN, Zwart P, Liang M, Boutet S, Robinson RC, and Neutze R

Subjects
Algorithms, Crystallography, X-Ray instrumentation, Crystallography, X-Ray methods, Image Processing, Computer-Assisted, Molecular Imaging instrumentation, Scattering, Radiation, Synchrotrons, X-Rays, Electrons, Lasers, Microtubules ultrastructure, Molecular Imaging methods, Tubulin ultrastructure
Abstract

X-ray free electron lasers (XFELs) create new possibilities for structural studies of biological objects that extend beyond what is possible with synchrotron radiation. Serial femtosecond crystallography has allowed high-resolution structures to be determined from micro-meter sized crystals, whereas single particle coherent X-ray imaging requires development to extend the resolution beyond a few tens of nanometers. Here we describe an intermediate approach: the XFEL imaging of biological assemblies with helical symmetry. We collected X-ray scattering images from samples of microtubules injected across an XFEL beam using a liquid microjet, sorted these images into class averages, merged these data into a diffraction pattern extending to 2 nm resolution, and reconstructed these data into a projection image of the microtubule. Details such as the 4 nm tubulin monomer became visible in this reconstruction. These results illustrate the potential of single-molecule X-ray imaging of biological assembles with helical symmetry at room temperature.

Published
2019
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13. From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography.

Author

Dods R, Båth P, Arnlund D, Beyerlein KR, Nelson G, Liang M, Harimoorthy R, Berntsen P, Malmerberg E, Johansson L, Andersson R, Bosman R, Carbajo S, Claesson E, Conrad CE, Dahl P, Hammarin G, Hunter MS, Li C, Lisova S, Milathianaki D, Robinson J, Safari C, Sharma A, Williams G, Wickstrand C, Yefanov O, Davidsson J, DePonte DP, Barty A, Brändén G, and Neutze R

Subjects
Bacterial Proteins chemistry, Crystallography, X-Ray, Hyphomicrobiaceae chemistry, Models, Molecular, Photosynthesis, Protein Conformation, Hyphomicrobiaceae metabolism, Membrane Proteins chemistry
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 vir ). We first crushed these crystals prior to multiple rounds of microseeding. Each cycle of microseeding facilitated improvements in the RC vir serial femtosecond crystallography (SFX) structure from 3.3-Å to 2.4-Å resolution. This approach may allow known crystallization conditions for other proteins to be adapted to exploit novel scientific opportunities created by serial crystallography., (Copyright © 2017 Elsevier Ltd. All rights reserved.)

Published
2017
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14. Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography.

Author

Johansson LC, Arnlund D, Katona G, White TA, Barty A, DePonte DP, Shoeman RL, Wickstrand C, Sharma A, Williams GJ, Aquila A, Bogan MJ, Caleman C, Davidsson J, Doak RB, Frank M, Fromme R, Galli L, Grotjohann I, Hunter MS, Kassemeyer S, Kirian RA, Kupitz C, Liang M, Lomb L, Malmerberg E, Martin AV, Messerschmidt M, Nass K, Redecke L, Seibert MM, Sjöhamn J, Steinbrener J, Stellato F, Wang D, Wahlgren WY, Weierstall U, Westenhoff S, Zatsepin NA, Boutet S, Spence JC, Schlichting I, Chapman HN, Fromme P, and Neutze R

Subjects
Protein Conformation, Crystallography, X-Ray methods, Hyphomicrobiaceae chemistry, Photosynthetic Reaction Center Complex Proteins chemistry
Abstract

Serial femtosecond crystallography is an X-ray free-electron-laser-based method with considerable potential to have an impact on challenging problems in structural biology. Here we present X-ray diffraction data recorded from microcrystals of the Blastochloris viridis photosynthetic reaction centre to 2.8 Å resolution and determine its serial femtosecond crystallography structure to 3.5 Å resolution. Although every microcrystal is exposed to a dose of 33 MGy, no signs of X-ray-induced radiation damage are visible in this integral membrane protein structure.

Published
2013
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