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Matrix (Stuttgart, Germany). Supplement|January 1, 1992
Structural basis for the action of thermolysinD E Tronrud, S L Roderick, B W MatthewsJournal of Molecular Biology|April 5, 1986
Structure and X-ray amino acid sequence of a bacteriochlorophyll A protein from Prosthecochloris aestuarii refined at 1.9 A resolutionD E Tronrud, M F Schmid, B W MatthewsEuropean Journal of Biochemistry|June 2, 1986
Crystallographic structural analysis of phosphoramidates as inhibitors and transition-state analogs of thermolysinD E Tronrud, A F Monzingo, B W MatthewsScience (New York, N.Y.)|January 30, 1987
Structures of two thermolysin-inhibitor complexes that differ by a single hydrogen bondD E Tronrud, H M Holden, B W MatthewsBiochemistry|January 4, 1983
Structural analysis of the inhibition of thermolysin by an active-site-directed irreversible inhibitorM A Holmes, D E Tronrud, B W MatthewsJournal of Molecular Biology|July 7, 1998
Refined structure of Cro repressor protein from bacteriophage lambda suggests both flexibility and plasticityD H Ohlendorf, D E Tronrud, B W MatthewsJournal of Molecular Biology|November 5, 1989
Contributions of left-handed helical residues to the structure and stability of bacteriophage T4 lysozymeH Nicholson, E Söderlind, D E Tronrud, et al.Biochemistry|April 20, 1993
Structure of the cobalt-dependent methionine aminopeptidase from Escherichia coli: a new type of proteolytic enzymeS L Roderick, B W MatthewsThe Journal of Biological Chemistry|November 15, 1988
Crystallization of methionine aminopeptidase from Escherichia coliS L Roderick, B W MatthewsBiopolymers|November 1, 1992
Analysis of the effectiveness of proline substitutions and glycine replacements in increasing the stability of phage T4 lysozymeH Nicholson, D E Tronrud, W J Becktel, et al.Pageof 20