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In-house SAD phasing with surface-bound cerium ions.

K Natesan Vennila¹, Devadasan Velmurugan

¹CAS in Crystallography and Biophysics, University of Madras, Maraimalai (Guindy) Campus, Chennai, Tamilnadu, India.

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications

|December 6, 2011

Summary

Cerium(III) ions in hen egg-white lysozyme (HEWL) crystals enabled macromolecular phasing using X-ray diffraction. This method accurately determined protein structure and revealed metal-ion interactions.

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Published on: January 25, 2020

Area of Science:

Structural Biology
Biophysics
Crystallography

Background:

Macromolecular phasing is crucial for determining protein structures.
Anomalous scattering techniques offer alternative phasing strategies.
Trivalent metal ions can serve as anomalous scatterers.

Purpose of the Study:

To utilize cerium(III) ions as anomalous scatterers for macromolecular phasing.
To determine the structure of hen egg-white lysozyme (HEWL) using single-wavelength anomalous diffraction (SAD).
To investigate the binding interactions of cerium(III) ions with HEWL.

Main Methods:

Crystallization of HEWL in the presence of cerium(III) chloride.
X-ray intensity data collection to 2 Å resolution using in-house Cu Kα radiation.
Single-wavelength anomalous scattering (SWS) phasing and automated structure solution using PHENIX software (AutoSol and AutoBuild).

Main Results:

A clearly interpretable electron-density map was obtained from single-wavelength data.
Automated substructure solution identified four cerium(III) sites.
Approximately 90% of the HEWL residues were automatically built into the electron density.
Cerium(III) ions were found to bind to the enzyme surface, interacting with carbonyl groups and water molecules.

Conclusions:

Cerium(III) ions can be effectively used as anomalous scatterers for macromolecular phasing.
In-house single-wavelength anomalous scattering (SWS) is a viable tool for protein structure determination.
This approach facilitates the study of trivalent metal ion interactions with proteins and other macromolecules.