Automated Protein Purification for Structural Studies

Autor: Thomas Pless, Jill A Sigrell, Hans O Andersson, Markus Galin, Lotta Hedqvist, Christine Markeland, Pia Liljedahl, Pär Eklund, Karin Torstenson
Rok vydání: 2018
Předmět:
Zdroj: The Scientific World Journal, Vol 2, Pp 33-34 (2002)
The Scientific World Journal
ISSN: 1537-744X
Popis: 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.
Databáze: OpenAIRE
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