Giuseppe Zaccai

Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway?

G Büldt, G. Zaccai, G. Büldt, 1990, Journal of molecular biology.

Mutation at a single acidic amino acid enhances the halophilic behaviour of malate dehydrogenase from Haloarcula marismortui in physiological salts.

D. Madern, G. Zaccai, C. Pfister, 1995, European journal of biochemistry.

Biochemical, structural, and molecular genetic aspects of halophilism.

H. Eisenberg, G. Zaccai, M. Mevarech, 1992, Advances in protein chemistry.

Biochemical and serological evidence for an RNase E-like activity in halophilic Archaea

B. Franzetti, G. Zaccai, B. Sohlberg, 1997, Journal of bacteriology.

Cloning, sequencing, and expression in Escherichia coli of the gene coding for malate dehydrogenase of the extremely halophilic archaebacterium Haloarcula marismortui.

H. Eisenberg, G. Zaccai, J. Chroboczek, 1993, Biochemistry.

Structural changes in bacteriorhodopsin during proton translocation revealed by neutron diffraction.

G. Zaccai, G. Büldt, N. Dencher, 1989, Proceedings of the National Academy of Sciences of the United States of America.

Stabilisation of halophilic malate dehydrogenase from Haloarcula marismortui by divalent cations -- effects of temperature, water isotope, cofactor and pH.

D. Madern, G. Zaccai, Giuseppe Zaccai, 1997, European journal of biochemistry.

Solution structure of halophilic malate dehydrogenase from small-angle neutron and X-ray scattering and ultracentrifugation.

E. Wachtel, H. Eisenberg, G. Zaccai, 1986, Journal of molecular biology.

Stability against denaturation mechanisms in halophilic malate dehydrogenase "adapt" to solvent conditions.

D. Madern, G. Zaccaı̈, F. Bonneté, 1994, Journal of molecular biology.