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Updated: Apr 6, 2026

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Single Particle Cryo-Electron Microscopy: From Sample to Structure

Published on: May 29, 2021

X-ray structure determination using low-resolution electron microscopy maps for molecular replacement.

Ryan N Jackson¹, Airlie J McCoy², Thomas C Terwilliger³

¹Department of Microbiology and Immunology, Montana State University, Bozeman, Montana, USA.

Nature Protocols

|July 31, 2015

Summary

This summary is machine-generated.

This study presents a protocol for integrating low-resolution electron microscopy (EM) maps with X-ray crystallography data. This method aids in determining high-resolution structures of macromolecular machines.

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Area of Science:

Structural Biology
Biophysics
Biochemistry

Background:

Macromolecular machine structures are typically determined by electron microscopy (EM) or X-ray crystallography.
EM provides low-resolution structures, while X-ray crystallography offers high-resolution details.
Integrating these techniques is crucial for atomic model generation of complexes.

Purpose of the Study:

To present a protocol for integrating low-resolution EM maps with X-ray crystallography data.
To overcome technical challenges in combining EM and X-ray diffraction data.
To facilitate the determination of high-resolution macromolecular structures.

Main Methods:

Placing low-resolution EM maps into the crystallographic unit cell using molecular replacement.
Computing initial phases from the placed EM density.
Extending phases to high resolution by averaging maps over noncrystallographic symmetry.

Main Results:

A step-by-step protocol for integrating EM and X-ray crystallography data is described.
The protocol enables the use of low-resolution EM maps to aid X-ray crystal structure determination.
The method effectively extends phase information from EM to high resolution.

Conclusions:

The presented protocol effectively integrates EM and X-ray crystallography data.
This integration method is becoming increasingly important as the resolution gap narrows.
The protocol will enhance the determination of atomic models for macromolecular complexes.