Automated Protein Purification for Structural Studies
Hans O. Andersson, Par Eklund, Markus Galin and 6 more
The Scientific World Journal · 2002
doi:10.1100/tsw.2002.17 (opens in a new tab)
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Abstract
INTRODUCTION. Structural genomics, also known as structural proteomics, aims to resolve protein functions on a large scale[1]. To determine structures using either X-ray crystallography or NMR, fairly large amounts (>10 mg) of target proteins (which are pure, homogenous, and concentrated) are usually required. A robust and easy-to-use protein purification scheme that can automatically produce numerous proteins in a desired form would increase the throughput of structure determination[2]. Using a new strategy and optimized methods, a newly configured AKTAexplorerTM (AKTA is a trademark of the Amersham Biosciences group. Amersham and Amersham Biosciences are trademarks of Amersham Plc. © Amersham Biosciences AB 2001 – All rights reserved.) 100 can perform automated two-step purification of up to six different proteins serially using two different purification schemes.
Abstract licence: CC BY
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