Automated Protein Purification for Structural Studies
Author(s) -
Hans O. Andersson,
Pär Eklund,
Markus Galin,
Lotta Hedqvist,
Pia Liljedahl,
Christine Markeland,
Thomas Pless,
Jill A. Sigrell,
Karin Torstenson
Publication year - 2002
Publication title -
the scientific world journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.453
H-Index - 93
eISSN - 2356-6140
pISSN - 1537-744X
DOI - 10.1100/tsw.2002.17
Subject(s) - computer science , computational biology , biology
. 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.
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