E. Köhler

A site-directed mutagenesis study to identify amino acid residues involved in the catalytic function of the restriction endonuclease EcoRV.

T. Oelgeschläger, A. Pingoud, J. Alves, 1992, Biochemistry.

DNA binding specificity of the EcoRV restriction endonuclease is increased by Mg2+ binding to a metal ion binding site distinct from the catalytic center of the enzyme.

A. Jeltsch, A. Pingoud, B. Connolly, 1995, Biochemistry.

Determination of the DNA bend angle induced by the restriction endonuclease EcoRV in the presence of Mg2+.

A. Pingoud, W. Wende, U. Fagin, 1993, The Journal of biological chemistry.

Crystallization and preliminary X-ray studies of an aspartate aminotransferase mutant from Escherichia coli.

K. Kirschner, J. Jansonius, U. Sauder, 1989, Journal of molecular biology.

Significant improvement to the catalytic properties of aspartate aminotransferase: role of hydrophobic and charged residues in the substrate binding pocket.

K. Kirschner, J. Jansonius, I. Fotheringham, 1994, Biochemistry.

Mg2+ confers DNA binding specificity to the EcoRV restriction endonuclease.

A. Pingoud, J. Alves, H. Wolfes, 1992, Biochemistry.

Site-directed mutagenesis studies with EcoRV restriction endonuclease to identify regions involved in recognition and catalysis.

F. Winkler, R. Geiger, A. Pingoud, 1991, Biochemistry.