Structure of the LexA Repressor−DNA Complex Probed by Affinity Cleavage and Affinity Photo-Cross-Linking-Reference-Cited by-同舟云学术

Structure of the LexA Repressor−DNA Complex Probed by Affinity Cleavage and Affinity Photo-Cross-Linking

Published:1996-01-01 Issue:14 Volume:35 Page:4279-4286
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Dumoulin Pascal¹,Ebright Richard H.¹,Knegtel Ronald¹,Kaptein Robert¹,Granger-Schnarr Michèle¹,Schnarr Manfred¹

Affiliation:

1. Institut de Biologie Moléculaire et Cellulaire, UPR 9002 du CNRS, 15 rue Descartes, F-67084 Strasbourg Cedex, France, Department of Chemistry and Waksman Institute, Rutgers University, New Brunswick, New Jersey 08855, and Bijvoet Center for Biomolecular Research, Utrecht University, Padualaan 8, 3584-CH Utrecht, The Netherlands

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi9529162

Reference55 articles.

1. Contacts between Tet repressor and tet operator revealed by new recognition specificities of single amino acid replacement mutants

2. Complex of lac repressor headpiece with a 14 base-pair lac operator fragment studied by two-dimensional nuclear magnetic resonance

3. Phenyl-azide-mediated Photocrosslinking Analysis of Cro-DNA Interaction

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