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Updated: Jun 21, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

Published on: January 10, 2018

Differences between CusA and AcrB crystallisation highlighted by protein flexibility.

Aurélien Deniaud¹, Aurélie Goulielmakis, Jacques Covès

¹Institut de Biologie Structurale Jean Pierre Ebel, UMR5075 CEA-CNRS-Université Joseph Fourier, Grenoble, France.

|July 14, 2009

Summary

This summary is machine-generated.

Researchers compared the Resistance Nodulation and cell Division (RND) transporter CusA to AcrB. Heavy metal cations were found to stabilize CusA, potentially aiding in its crystallization.

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Last Updated: Jun 21, 2026

Combining X-Ray Crystallography with Small Angle X-Ray Scattering to Model Unstructured Regions of Nsa1 from S. Cerevisiae

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Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering

Growing Protein Crystals with Distinct Dimensions Using Automated Crystallization Coupled with In Situ Dynamic Light Scattering

Published on: August 14, 2018

Area of Science:

Structural biology
Membrane transport proteins

Background:

AcrB is a well-characterized Resistance Nodulation and cell Division (RND) transporter.
Limited structural data exists for other RND transporters like CusA.

Purpose of the Study:

To compare the structural properties of CusA and AcrB.
To identify factors that may influence CusA crystallization.

Main Methods:

Limited proteolysis assays to assess protein dynamics.
Crystallization trials of CusA and AcrB in dodecylmaltoside.
Investigating the effect of various compounds, including heavy metal cations, on CusA stability.

Main Results:

AcrB crystallized readily, while CusA did not under similar conditions.
Limited proteolysis indicated differences in protein dynamics between AcrB and CusA.
Heavy metal cations stabilized CusA, suggesting a potential method for improving crystallization.

Conclusions:

Differences in dynamics may explain the varying crystallization behavior of CusA and AcrB.
Stabilization of CusA by heavy metal cations is a promising first step towards achieving its crystallization.