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Preparation of Samples for Electron Microscopy01:20

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To be visualized by an electron microscope, either transmission or scanning, biological samples need to be fixed (stabilized) so the electron beam does not destroy them and dried thoroughly (desiccated/dehydrated) so the vacuum does not affect them. Fixation needs to be done as quickly as possible because the sample properties will start changing as soon as it is removed from its natural environment. For example, in a tissue sample, the oxygen levels begin decreasing, causing an altered...
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Fixed Target Serial Data Collection at Diamond Light Source
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Standard Sample Preparation for Serial Femtosecond Crystallography.

Christina Schmidt1, Kristina Lorenzen1, Joachim Schulz1

  • 1European XFEL GmbH, Holzkoppel 4, 22869 Schenefeld, Germany.

Biomolecules
|November 27, 2025
PubMed
Summary
This summary is machine-generated.

This review details standard proteins and microcrystal preparation for serial crystallography (SX), including serial synchrotron crystallography (SSX) and serial femtosecond crystallography (SFX). It offers practical guidance for reproducible biomolecular structure determination at X-ray Free Electron Lasers (XFELs).

Keywords:
microcrystalsprotocolserial femtosecond crystallographystandard samples

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Area of Science:

  • Structural Biology
  • Biophysics
  • Crystallography

Background:

  • Serial crystallography (SX), encompassing serial synchrotron crystallography (SSX) and serial femtosecond crystallography (SFX), enables high-resolution biomolecular structure determination from microcrystals at room temperature.
  • Standardized protein samples are crucial for validating new X-ray Free Electron Laser (XFEL) instruments and experimental setups.

Purpose of the Study:

  • To review commonly used standard proteins for SX experiments.
  • To present optimized microcrystal preparation workflows for four model systems: lysozyme, myoglobin, iq-mEmerald, and photoactive yellow protein (PYP).
  • To provide practical guidance for the serial crystallography community to enhance reproducibility and experimental consistency.

Main Methods:

  • Literature review of established methodologies for standard protein sample preparation.
  • Description of microcrystal preparation workflows based on experimental experience at the European XFEL.
  • Consolidation of refined and optimized protocols for lysozyme, myoglobin, iq-mEmerald, and PYP.

Main Results:

  • Identification and summary of widely adopted standard proteins for SX.
  • Detailed workflows for preparing microcrystals of lysozyme, myoglobin, iq-mEmerald, and PYP.
  • Integration of practical insights and optimized protocols for routine SX applications.

Conclusions:

  • The review provides essential guidance for selecting and preparing standard protein samples for serial crystallography.
  • Optimized protocols contribute to enhanced reproducibility and reliable experimental performance at XFEL facilities.
  • This work supports the broader scientific community in advancing structural biology through serial crystallography techniques.