Purification and Polishing His-Tagged Proteins for Crystallography

Purifying His-Tagged Proteins with Vivapure^® IEX

Scouting and Preparative Purification of His-Tagged Proteins Application Note

Authors: Dr. Mark McAlister, John Phelan and Dr. Roberto Sarra | Last updated: June 2021

Overview

The structure of a protein influences its function and how it interacts with other molecules. Therefore, structural biology plays a crucial role in the design of novel drugs.

Common structure determination methods, such as x-ray crystallography, require the preparation of proteins to high purity and at relatively large quantities. Ion exchange chromatography is a ubiquitous, cost-effective, and easy method for protein purification.

In this application note, we introduce Vivapure^® and Sartobind^® solutions to demonstrate the simplicity, efficiency and relevance of Sartobind^® membrane adsorbers from scouting to preparative purification.

Document type: Application Note
Page count: 6
Read time: 8 minutes

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Key Takeaways

The significance of protein purification in structural biology laboratories
Ion exchange chromatography as an alternative to metal affinity purification
Methods and buffers used for a scouting purification process with Vivapure^® IEX
Scale up to preparative purification using the same Sartobind membrane adsorber technology

This Resource is Designed for:

Researchers in laboratories using protein expression and purification for structural and functional analyses

Applications Supported:

Scouting purification
Preparative purification
His-tagged protein purification
Ion exchange chromatography