The Experts below are selected from a list of 306 Experts worldwide ranked by ideXlab platform

Garth J. Williams - One of the best experts on this subject based on the ideXlab platform.

  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    2016
    Co-Authors: Linda C. Johansson, Gergely Katona, David Arnlund, Thomas A. White, Daniel P. Deponte, Robert L. Shoeman, Anton Barty, Cecilia Wickstr, Amit Sharma, Garth J. Williams
    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 2.8Å resolution and determine its serial femtosecond crystallography structure to 3.5Å resolution. Although every microcrystal is exposed to a dose of 33MGy, no signs of X-ray-induced radiation damage are visible in this integra

  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    Nature communications, 2013
    Co-Authors: Linda C. Johansson, Gergely Katona, David Arnlund, Cecilia Wickstrand, Thomas A. White, Daniel P. Deponte, Robert L. Shoeman, Anton Barty, Amit Sharma, Garth J. Williams
    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 A resolution and determine its serial femtosecond crystallography structure to 3.5 A 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.

  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    Nature Communications, 2013
    Co-Authors: Linda C. Johansson, Gergely Katona, David Arnlund, Cecilia Wickstrand, Thomas A. White, Daniel P. Deponte, Robert L. Shoeman, Anton Barty, Amit Sharma, Garth J. Williams
    Abstract:

    Serial femtosecond crystallography is an X-ray free-electron-laser-based method that uses X-ray bursts to determine protein structures. Here the authors present the structure of a photosynthetic reaction centre, an integral membrane protein, achieved with no sign of X-ray-induced radiation damage. 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.

Linda C. Johansson - One of the best experts on this subject based on the ideXlab platform.

  • From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography
    Structure (London England : 1993), 2017
    Co-Authors: Robert Dods, Petra Båth, David Arnlund, Erik Malmerberg, Kenneth R. Beyerlein, Garrett Nelson, Mengling Liang, Rajiv Harimoorthy, Peter Berntsen, Linda C. Johansson
    Abstract:

    Summary 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-A to 2.4-A resolution. This approach may allow known crystallization conditions for other proteins to be adapted to exploit novel scientific opportunities created by serial crystallography.

  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    2016
    Co-Authors: Linda C. Johansson, Gergely Katona, David Arnlund, Thomas A. White, Daniel P. Deponte, Robert L. Shoeman, Anton Barty, Cecilia Wickstr, Amit Sharma, Garth J. Williams
    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 2.8Å resolution and determine its serial femtosecond crystallography structure to 3.5Å resolution. Although every microcrystal is exposed to a dose of 33MGy, no signs of X-ray-induced radiation damage are visible in this integra

  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    Nature communications, 2013
    Co-Authors: Linda C. Johansson, Gergely Katona, David Arnlund, Cecilia Wickstrand, Thomas A. White, Daniel P. Deponte, Robert L. Shoeman, Anton Barty, Amit Sharma, Garth J. Williams
    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 A resolution and determine its serial femtosecond crystallography structure to 3.5 A 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.

  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    Nature Communications, 2013
    Co-Authors: Linda C. Johansson, Gergely Katona, David Arnlund, Cecilia Wickstrand, Thomas A. White, Daniel P. Deponte, Robert L. Shoeman, Anton Barty, Amit Sharma, Garth J. Williams
    Abstract:

    Serial femtosecond crystallography is an X-ray free-electron-laser-based method that uses X-ray bursts to determine protein structures. Here the authors present the structure of a photosynthetic reaction centre, an integral membrane protein, achieved with no sign of X-ray-induced radiation damage. 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.

Robert Kostecki - One of the best experts on this subject based on the ideXlab platform.

  • ir near field spectroscopy and imaging of single lixfepo4 Microcrystals
    Nano Letters, 2015
    Co-Authors: Ivan Thomas Lucas, A. S. Mcleod, Jaroslaw Syzdek, D. S. Middlemiss, C. P. Grey, D. N. Basov, Robert Kostecki
    Abstract:

    This study demonstrates the unique capability of infrared near-field nanoscopy combined with Fourier transform infrared spectroscopy to map phase distributions in Microcrystals of LixFePO4, a positive electrode material for Li-ion batteries. Ex situ nanoscale IR imaging provides direct evidence for the coexistence of LiFePO4 and FePO4 phases in partially delithiated single-crystal microparticles. A quantitative three-dimensional tomographic reconstruction of the phase distribution within a single microcrystal provides new insights into the phase transformation and/or relaxation mechanism, revealing a FePO4 shell surrounding a diamond-shaped LiFePO4 inner core, gradually shrinking in size and vanishing upon delithiation of the crystal. The observed phase propagation pattern supports recent functional models of LiFePO4 operation relating electrochemical performance to material design. This work demonstrates the remarkable potential of near-field optical techniques for the characterization of electrochemical...

  • IR Near-Field Spectroscopy and Imaging of Single LixFePO4 Microcrystals
    Nano Letters, 2015
    Co-Authors: Ivan Thomas Lucas, A. S. Mcleod, Jaroslaw Syzdek, D. S. Middlemiss, C. P. Grey, D. N. Basov, Robert Kostecki
    Abstract:

    This study demonstrates the unique capability of infrared near-field nanoscopy combined with Fourier transform infrared spectroscopy to map phase distributions in Microcrystals of LixFePO4, a positive electrode material for Li-ion batteries. Ex situ nanoscale IR imaging provides direct evidence for the coexistence of LiFePO4 and FePO4 phases in partially delithiated single-crystal microparticles. A quantitative three-dimensional tomographic reconstruction of the phase distribution within a single microcrystal provides new insights into the phase transformation and/or relaxation mechanism, revealing a FePO4 shell surrounding a diamond-shaped LiFePO4 inner core, gradually shrinking in size and vanishing upon delithiation of the crystal. The observed phase propagation pattern supports recent functional models of LiFePO4 operation relating electrochemical performance to material design. This work demonstrates the remarkable potential of near-field optical techniques for the characterization of electrochemical materials and interfaces.

David Arnlund - One of the best experts on this subject based on the ideXlab platform.

  • From Macrocrystals to Microcrystals: A Strategy for Membrane Protein Serial Crystallography
    Structure (London England : 1993), 2017
    Co-Authors: Robert Dods, Petra Båth, David Arnlund, Erik Malmerberg, Kenneth R. Beyerlein, Garrett Nelson, Mengling Liang, Rajiv Harimoorthy, Peter Berntsen, Linda C. Johansson
    Abstract:

    Summary 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-A to 2.4-A resolution. This approach may allow known crystallization conditions for other proteins to be adapted to exploit novel scientific opportunities created by serial crystallography.

  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    2016
    Co-Authors: Linda C. Johansson, Gergely Katona, David Arnlund, Thomas A. White, Daniel P. Deponte, Robert L. Shoeman, Anton Barty, Cecilia Wickstr, Amit Sharma, Garth J. Williams
    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 2.8Å resolution and determine its serial femtosecond crystallography structure to 3.5Å resolution. Although every microcrystal is exposed to a dose of 33MGy, no signs of X-ray-induced radiation damage are visible in this integra

  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    Nature communications, 2013
    Co-Authors: Linda C. Johansson, Gergely Katona, David Arnlund, Cecilia Wickstrand, Thomas A. White, Daniel P. Deponte, Robert L. Shoeman, Anton Barty, Amit Sharma, Garth J. Williams
    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 A resolution and determine its serial femtosecond crystallography structure to 3.5 A 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.

  • Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography
    Nature Communications, 2013
    Co-Authors: Linda C. Johansson, Gergely Katona, David Arnlund, Cecilia Wickstrand, Thomas A. White, Daniel P. Deponte, Robert L. Shoeman, Anton Barty, Amit Sharma, Garth J. Williams
    Abstract:

    Serial femtosecond crystallography is an X-ray free-electron-laser-based method that uses X-ray bursts to determine protein structures. Here the authors present the structure of a photosynthetic reaction centre, an integral membrane protein, achieved with no sign of X-ray-induced radiation damage. 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.

Ivan Thomas Lucas - One of the best experts on this subject based on the ideXlab platform.

  • ir near field spectroscopy and imaging of single lixfepo4 Microcrystals
    Nano Letters, 2015
    Co-Authors: Ivan Thomas Lucas, A. S. Mcleod, Jaroslaw Syzdek, D. S. Middlemiss, C. P. Grey, D. N. Basov, Robert Kostecki
    Abstract:

    This study demonstrates the unique capability of infrared near-field nanoscopy combined with Fourier transform infrared spectroscopy to map phase distributions in Microcrystals of LixFePO4, a positive electrode material for Li-ion batteries. Ex situ nanoscale IR imaging provides direct evidence for the coexistence of LiFePO4 and FePO4 phases in partially delithiated single-crystal microparticles. A quantitative three-dimensional tomographic reconstruction of the phase distribution within a single microcrystal provides new insights into the phase transformation and/or relaxation mechanism, revealing a FePO4 shell surrounding a diamond-shaped LiFePO4 inner core, gradually shrinking in size and vanishing upon delithiation of the crystal. The observed phase propagation pattern supports recent functional models of LiFePO4 operation relating electrochemical performance to material design. This work demonstrates the remarkable potential of near-field optical techniques for the characterization of electrochemical...

  • IR Near-Field Spectroscopy and Imaging of Single LixFePO4 Microcrystals
    Nano Letters, 2015
    Co-Authors: Ivan Thomas Lucas, A. S. Mcleod, Jaroslaw Syzdek, D. S. Middlemiss, C. P. Grey, D. N. Basov, Robert Kostecki
    Abstract:

    This study demonstrates the unique capability of infrared near-field nanoscopy combined with Fourier transform infrared spectroscopy to map phase distributions in Microcrystals of LixFePO4, a positive electrode material for Li-ion batteries. Ex situ nanoscale IR imaging provides direct evidence for the coexistence of LiFePO4 and FePO4 phases in partially delithiated single-crystal microparticles. A quantitative three-dimensional tomographic reconstruction of the phase distribution within a single microcrystal provides new insights into the phase transformation and/or relaxation mechanism, revealing a FePO4 shell surrounding a diamond-shaped LiFePO4 inner core, gradually shrinking in size and vanishing upon delithiation of the crystal. The observed phase propagation pattern supports recent functional models of LiFePO4 operation relating electrochemical performance to material design. This work demonstrates the remarkable potential of near-field optical techniques for the characterization of electrochemical materials and interfaces.