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Related Experiment Videos

Low-dose fixed-target serial synchrotron crystallography.

Robin L Owen1, Danny Axford1, Darren A Sherrell1

  • 1Diamond Light Source, Harwell Science and Innovation Campus, Didcot OX11 0DE, England.

Acta Crystallographica. Section D, Structural Biology
|April 5, 2017
PubMed
Summary

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This summary is machine-generated.

Serial crystallography, driven by X-ray free-electron lasers, is now advancing synchrotron capabilities. A fixed-target method enables high-throughput serial data collection for room-temperature, low-dose protein structure determination with minimal sample use.

Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Serial crystallography techniques were initially developed to meet the stringent sample requirements of X-ray free-electron lasers (XFELs).
  • These advanced serial methods are increasingly being adapted and utilized at synchrotron radiation sources.
  • Efficient data collection from micro- or nano-crystals remains a challenge in serial crystallography.

Purpose of the Study:

  • To demonstrate the feasibility of high-throughput serial data collection at synchrotrons using a fixed-target approach.
  • To determine the room-temperature, low-dose structure of myoglobin crystals.
  • To assess the efficiency and sample consumption of the fixed-target serial crystallography method.

Main Methods:

  • Development and implementation of a fixed-target array system for serial sample delivery.
Keywords:
crystallography on a chipfixed targetlow dosemacromolecular crystallographyroom-temperature crystallographyserial synchrotron crystallography

Related Experiment Videos

  • Integration of a high-speed, precise translation stage for crystal manipulation.
  • Data collection from myoglobin microcrystals at a synchrotron source.
  • Application of serial crystallography data processing and structure determination algorithms.

    • Main Results:

    • High-quality crystallographic data were successfully collected from myoglobin crystals using the fixed-target serial approach.
    • Room-temperature, low-dose structure determination of myoglobin was achieved, demonstrating the method's potential.
    • The combination of fixed-target arrays and advanced translation systems enabled high hit rates.
    • The method proved to be highly efficient in terms of sample consumption.

    Conclusions:

    • The fixed-target serial crystallography approach is a viable and powerful technique for high-throughput data collection at synchrotrons.
    • This method facilitates room-temperature, low-dose structural studies, overcoming limitations of previous techniques.
    • The demonstrated efficiency and low sample requirement pave the way for broader applications in structural biology.