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Related Concept Videos

Determination of Crystal Structures01:29

Determination of Crystal Structures

122
In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...
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X-ray Crystallography02:18

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The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...
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Related Experiment Video

Updated: Apr 15, 2026

Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography
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Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography

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Lipidic cubic phase serial millisecond crystallography using synchrotron radiation.

Przemyslaw Nogly1, Daniel James2, Dingjie Wang2

  • 1Laboratory for Biomolecular Research, Paul Scherrer Institute, Villigen 5232, Switzerland.

Iucrj
|April 14, 2015
PubMed
Summary
This summary is machine-generated.

Serial millisecond crystallography (SMX) using lipidic cubic phases (LCPs) enables room-temperature membrane protein structure determination. This method advances structural biology by simplifying crystal handling and data collection at synchrotrons.

Keywords:
XFELbacteriorhodopsinlipidic cubic phasesprotein crystallography

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Lipidico Injection Protocol for Serial Crystallography Measurements at the Australian Synchrotron
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Lipidico Injection Protocol for Serial Crystallography Measurements at the Australian Synchrotron
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Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Lipidic cubic phases (LCPs) are effective matrices for membrane protein crystallization.
  • LCPs serve as a delivery medium for serial femtosecond crystallography (SFX) at X-ray free-electron lasers (XFELs).

Purpose of the Study:

  • To adapt LCP-based serial crystallography for synchrotron microfocus beamlines, enabling serial millisecond crystallography (SMX).
  • To demonstrate the utility of LCP-SMX for room-temperature structure determination of membrane proteins.

Main Methods:

  • Adaptation of lipidic cubic phase (LCP) technology for serial millisecond crystallography (SMX).
  • Utilizing synchrotron microfocus beamlines for LCP-SMX data collection.
  • Structure determination of bacteriorhodopsin (bR) at room temperature.

Main Results:

  • Successful implementation of LCP-SMX at synchrotron microfocus beamlines.
  • Elimination of difficult individual crystal handling required in conventional microcrystallography.
  • Room-temperature structure of bacteriorhodopsin (bR) solved at 2.4 Å resolution.

Conclusions:

  • LCP-SMX is a viable technique for room-temperature membrane protein structure determination using widely available synchrotron sources.
  • The method simplifies crystal handling and data collection compared to conventional techniques.
  • Observed room-temperature structural differences in bR highlight the importance of temperature in structural studies.