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PEDS Advance Access originally published online on August 27, 2004
Protein Engineering Design and Selection 2004 17(7):553-555; doi:10.1093/protein/gzh069
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Protein Engineering, Design & Selection vol. 17 no. 7 © Oxford University Press 2004; all rights reserved

COMMUNICATION

A thermostable enzyme as an experimental platform to study properties of less stable homologues

Holger Lill1, Toru Hisabori2, Georg Groth3 and Dirk Bald1,4

1Department of Structural Biology, Faculty of Earth and Life Science, De Boelelaan 1085, 1081 HV Amsterdam, The Netherlands, 2Chemical Resources Laboratory, Tokyo Institute of Technology, Nagatsuta 4259, Yokohama 226-8503, Japan and 3Department of Plant Biochemistry, University of Düsseldorf, Universitätsstrasse 1, 40225 Düsseldorf, Germany

4 To whom correspondence should be addressed. E-mail: dirk.bald{at}falw.vu.nl

The structural and functional characterization of proteins is frequently hampered by lack of stability or by insufficient assembly of oligomeric proteins in over-expression systems. Using F1-ATPase as a case study, we tackled this problem by introducing function-determining domains from a difficult-to-handle variety of an enzyme into a stable homologue.

Received March 29, 2004; revised June 24, 2004; accepted August 12, 2004.

Edited by Luis Serrano


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