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Related Experiment Video

Updated: Jan 19, 2026

Improving High Viscosity Extrusion of Microcrystals for Time-resolved Serial Femtosecond Crystallography at X-ray Lasers
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Liquid application method for time-resolved analyses by serial synchrotron crystallography.

Pedram Mehrabi1, Eike C Schulz1,2, Michael Agthe3

  • 1Max-Planck-Institute for Structure and Dynamics of Matter, Department for Atomically Resolved Dynamics, Hamburg, Germany.

Nature Methods
|September 19, 2019
PubMed
Summary
This summary is machine-generated.

We developed a new method for time-resolved analyses (LAMA) using liquid droplets for faster protein studies. This technique rapidly binds ligands to crystals, enabling detailed analysis of molecular interactions.

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Last Updated: Jan 19, 2026

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Crystallography

Background:

  • Time-resolved crystallography requires rapid mixing of ligands with protein crystals.
  • Existing methods face challenges in achieving rapid and complete ligand binding.

Purpose of the Study:

  • Introduce a novel liquid application method for time-resolved analyses (LAMA).
  • Enable near-instantaneous ligand binding to protein crystals for in situ studies.

Main Methods:

  • Developed LAMA, an in situ mixing technique using picoliter droplets.
  • Applied LAMA to chip-mounted protein crystals for time-resolved experiments.

Main Results:

  • Achieved near-full ligand occupancy within theoretical diffusion times.
  • Demonstrated GlcNAc binding to lysozyme.
  • Resolved glucose binding and ring opening in xylose isomerase using time-resolved analysis.

Conclusions:

  • LAMA is a powerful tool for time-resolved structural biology.
  • The method facilitates rapid kinetic studies of ligand-protein interactions.