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Related Experiment Video

Updated: Feb 16, 2026

Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling

Contrast-Matching Detergent in Small-Angle Neutron Scattering Experiments for Membrane Protein Structural Analysis and Ab Initio Modeling

Published on: October 21, 2018

Direct from the seed: an atomic resolution protein structure by ab initio MicroED.

Purna Chandra Rao Vasireddy¹, Timothy Low-Beer¹, Katherine A Spoth^1,2

¹Department of Structural Biology, Jacobs School of Medicine and Biomedical Sciences, University at Buffalo, The State University of New York, Buffalo, NY, USA.

Nature Communications

|February 14, 2026

Summary

Researchers achieved atomic resolution protein structures using microcrystal electron diffraction (MicroED). This method, applied to the crambin protein, successfully solved the structure ab initio, providing a new benchmark for high-resolution electron crystallography.

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Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

Protein structure determination is crucial for understanding biological function.
Microcrystal electron diffraction (MicroED) offers a promising alternative to X-ray crystallography for small or sensitive crystals.
Challenges remain in achieving high resolution and solving structures ab initio with MicroED.

Purpose of the Study:

To determine the atomic resolution structure of the seed protein crambin using MicroED.
To establish a benchmark for ab initio structure solution with MicroED.
To demonstrate the effectiveness of serial merging and anisotropy correction for MicroED data.

Main Methods:

Spontaneous formation of protein nanocrystals from ethanolic purification drops.
Data collection using microcrystal electron diffraction (MicroED) on 58 nanocrystals.
Serial merging of diffraction data and anisotropy aware truncation.
Ab initio structure solution using a five-residue helical fragment for phasing.

Main Results:

An atomic resolution (0.85 Å) MicroED structure of crambin was solved ab initio.
Automated model building and resolution of individual hydrogen atoms were achieved.
The study demonstrates successful sub-ångström resolution MicroED without specialized equipment.

Conclusions:

Protein nanocrystals suitable for MicroED can be readily obtained.
Serial merging combined with anisotropy correction enables ab initio MicroED structure solution.
This work provides a benchmark for high-resolution MicroED on standard instrumentation.