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Related Concept Videos

Determination of Crystal Structures01:29

Determination of Crystal Structures

69
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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X-ray Diffraction of Biological Samples01:10

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X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
According to Bragg's law, when X-rays strike the sample positioned on a stage, the rays are  scattered by the electron clouds around the sample atoms. The  X-ray diffraction or scattering is caused by constructive interference of the X-ray waves that reflect off the internal...
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Related Experiment Video

Updated: Mar 25, 2026

Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092
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Biochemical and Structural Characterization of the Carbohydrate Transport Substrate-binding-protein SP0092

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Protein crystal structure from non-oriented, single-axis sparse X-ray data.

Jennifer L Wierman1, Ti-Yen Lan2, Mark W Tate2

  • 1Field of Biophysics, Cornell University, Ithaca, NY 14853, USA; Cornell High Energy Synchrotron Source (CHESS), Cornell University, Ithaca, NY 14853, USA.

Iucrj
|February 13, 2016
PubMed
Summary
This summary is machine-generated.

Serial femtosecond crystallography (SFX) advances protein structure determination. A new algorithm reconstructs 3D diffraction data from sparse synchrotron radiation frames, enabling structure solution without conventional Bragg peaks.

Keywords:
EMC algorithmX-ray serial microcrystallographyprotein microcrystallographysparse datasynchrotron-radiation sources

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Area of Science:

  • Structural Biology
  • Crystallography
  • Biophysics

Background:

  • Serial femtosecond crystallography (SFX) utilizes X-ray free-electron lasers (XFELs) for protein structure determination.
  • SFX involves collecting diffraction data from microcrystals exposed to ultrashort X-ray pulses.
  • Interest is growing in adapting SFX principles to synchrotron radiation (SR) sources.

Purpose of the Study:

  • To demonstrate the feasibility of reconstructing 3D diffraction intensity from sparse data collected at SR sources.
  • To validate the use of the EMC algorithm in a challenging sparsity regime.
  • To enable protein structure solution using SR-based serial crystallography.

Main Methods:

  • Simulated diffraction patterns from a rotating hen egg-white lysozyme (HEWL) crystal using an X-ray generator.
  • Recorded millions of sparse diffraction frames with a fast-framing detector.
  • Applied the EMC algorithm for data reconstruction without prior knowledge of crystal orientation.

Main Results:

  • Successfully reconstructed 3D diffraction intensity from extremely sparse frames (∼200 photons/frame).
  • Demonstrated feasibility even without detectable Bragg peaks for orientation determination.
  • The reconstructed data were phased and refined to solve the HEWL protein structure.

Conclusions:

  • The EMC algorithm enables practical synchrotron-based serial crystallography with micrometre-sized crystals.
  • Protein structure solution is achievable even with highly sparse diffraction data.
  • This method expands the accessibility of advanced crystallography techniques.