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Related Experiment Video

Updated: Jan 22, 2026

Preparation and Delivery of Protein Microcrystals in Lipidic Cubic Phase for Serial Femtosecond Crystallography
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Sulfur-SAD phasing from microcrystals utilizing low-energy X-rays.

Zbigniew Dauter1

  • 1National Cancer Institute, Argonne National Laboratory, Argonne, IL 60439, USA.

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|July 19, 2019
PubMed
Summary
This summary is machine-generated.

This study presents a practical method for collecting single-wavelength anomalous diffraction (S-SAD) data from native protein microcrystals using low-wavelength synchrotron radiation, advancing crystallographic structure determination.

Keywords:
S-SADanomalous diffractionlow-energy X-raysmicrocrystalsmicrodiffractionmultiple crystalsnative SADradiation damage

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Area of Science:

  • Structural Biology
  • Crystallography
  • Biophysics

Background:

  • Native protein microcrystals are challenging for X-ray diffraction.
  • Low-wavelength synchrotron radiation offers advantages for data collection.
  • Single-wavelength anomalous diffraction (SAD) is a powerful phasing technique.

Purpose of the Study:

  • To present a practical protocol for S-SAD data collection.
  • To enable structure determination from native protein microcrystals.
  • To utilize low-wavelength synchrotron radiation effectively.

Main Methods:

  • Application of a practical approach for S-SAD data acquisition.
  • Utilizing native protein microcrystals.
  • Employing low-wavelength synchrotron radiation.

Main Results:

  • Successful collection of S-SAD data from native protein microcrystals.
  • Demonstration of a viable method for crystallographic phasing.
  • Advancement in the practical application of synchrotron radiation.

Conclusions:

  • The presented approach facilitates S-SAD data collection from challenging samples.
  • This method expands the utility of synchrotron radiation in structural biology.
  • Enables routine structure determination of proteins from microcrystals.