• Publications
  • Influence
Solvent content of protein crystals.
  • B. Matthews
  • Chemistry
    Journal of molecular biology
  • 28 April 1968
Response of a protein structure to cavity-creating mutations and its relation to the hydrophobic effect.
Six "cavity-creating" mutants were constructed within the hydrophobic core of phage T4 lysozyme and the results suggest how to reconcile a number of conflicting reports concerning the strength of thehydrophobic effect in proteins.
An efficient general-purpose least-squares refinement program for macromolecular structures
A package of programs has been developed for efficient restrained least-squares refinement of macromolecular crystal structures. The package has been designed to be as flexible and general purpose as
Accurate calculation of the density of proteins.
The Voronoi algorithm is used to calculate the mean atomic volume for 30 representative protein structures and it is shown that this criterion is not sufficiently restrictive to ensure accurate volume determinations.
Structural basis for the attachment of a paramyxoviral polymerase to its template.
This study provides a structural analysis of polymerase-template interactions in a paramyxovirus and presents an example of a protein-protein interaction that must be only transiently maintained as part of its normal function.
The helix-turn-helix DNA binding motif.
Escherichia coli biotin holoenzyme synthetase/bio repressor crystal structure delineates the biotin- and DNA-binding domains.
The three-dimensional structure of BirA, the repressor of the Escherichia coli biotin biosynthetic operon, has been determined by x-ray crystallography and refined to a crystallographic residual of
Structure and function of the methionine aminopeptidases.