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Related Experiment Video

Updated: Sep 21, 2025

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Structural Studies of Macromolecules in Solution using Small Angle X-Ray Scattering

Published on: November 5, 2018

Ab initio phasing macromolecular structures using electron-counted MicroED data.

Michael W Martynowycz^1,2, Max T B Clabbers², Johan Hattne^1,2

¹Howard Hughes Medical Institute, University of California, Los Angeles, CA, USA.

|May 31, 2022

Summary

This summary is machine-generated.

This study demonstrates ab initio protein structure determination using microcrystal electron diffraction (MicroED). High-resolution macromolecular structures were solved using electron counting data and ab initio phasing, advancing structural biology.

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Last Updated: Sep 21, 2025

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Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

Determining high-resolution protein structures is crucial for understanding biological function.
Microcrystal electron diffraction (MicroED) offers a promising alternative for small or difficult-to-crystallize samples.

Purpose of the Study:

To determine protein structures ab initio using MicroED data.
To demonstrate the feasibility of ab initio phasing with electron counting data.

Main Methods:

Microcrystal electron diffraction (MicroED) data collection in counting mode.
Scanning electron microscopy (SEM) for microcrystal identification.
Focused ion beam (FIB) thinning for sample preparation.
Ab initio phasing using initial phase information from small fragments and density modification.

Main Results:

Atomic resolution (0.87 Å) structure of triclinic lysozyme determined ab initio.
Sub-ångström resolution (1.5 Å) structure of proteinase K determined using a similar approach.
Successful ab initio phasing demonstrated on electron counting MicroED data.

Conclusions:

Macromolecular structures can be determined to sub-ångström resolution by MicroED.
Ab initio phasing is a viable strategy for MicroED data, especially with electron counting.
This method advances the field of structural biology for challenging protein samples.