Daniel W. Kneller

Mutations at the Cysteine Codons of the recA Gene of Escherichia coli

MODEL FOR A DNA MEDIATED SYNAPTIC COMPLEX SUGGESTED BY CRYSTAL PACKING OF GAMMA DELTA RESOLVASE SUBUNITS

Hydrophilic-interaction chromatography for the separation of peptides, nucleic acids and other polar compounds

Structure of the recA protein–ADP complex

The RecA Protein: Structure and Functio

The structure of the E. coli recA protein monomer and polymer

The crystal structure of the Thermus aquaticus DnaB helicase monomer

Structure at 2.8 Â resolution of F1-ATPase from bovine heart mitochondria

Evidence for nucleotide-mediated changes in the domain structure of the RecA protein of Escherichia coli

Structural Relationship of Bacterial RecA Proteins to Recombination Proteins from Bacteriophage T4 and Yeast

New recA mutations that dissociate the various RecA protein activities in Escherichia coli provide evidence for an additional role for RecA protein in UV mutagenesis

Construction of a recombinase-deficient mutant recA protein that retains single-stranded DNA-dependent ATPase activity.

High-performance hydrophobic-interaction chromatography of proteins on a series of poly(alkyl aspart-amide)-silicas

Location of functional regions of the Escherichia coli RecA protein by DNA sequence analysis of RecA protease-constitutive mutants

Protein-protein interactions directing resolvase site-specific recombination: a structure-function analysis.

A Model for the Core Structure of the Escherichia coli RecA Protein