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Journal of Bacteriology, February 2008, p. 1484-1487, Vol. 190, No. 4
0021-9193/08/$08.00+0 doi:10.1128/JB.01488-07
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Department of Biochemistry, University of Wisconsin—Madison, Madison, Wisconsin 53706,1 The Josephine Bay Paul Center, The Marine Biology Laboratory, Woods Hole, Massachusetts 025432
Received 14 September 2007/ Accepted 4 December 2007
A series of Tn5 transposases (Tnp's) with mutations at the conserved amino acid position W450, which was structurally predicted to be important for synapsis, have been generated and characterized. This study demonstrates that W450 is involved in hydrophobic (and possibly aromatic) contacts within the Tnp monomer that negatively regulate synaptic complex formation.
Published ahead of print on 14 December 2007.
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