R Ladenstein

Ion pairs and the thermotolerance of proteins from hyperthermophiles: a "traffic rule" for hot roads.

A. Karshikoff, R. Ladenstein, A. Karshikoff, 2001, Trends in biochemical sciences.

Proteins from hyperthermophiles: stability and enzymatic catalysis close to the boiling point of water.

R. Ladenstein, G. Antranikian, R Ladenstein, 1998, Advances in biochemical engineering/biotechnology.

X-ray structure analysis and crystallographic refinement of lumazine synthase from the hyperthermophile Aquifex aeolicus at 1.6 A resolution: determinants of thermostability revealed from structural comparisons.

A. Bacher, R. Ladenstein, X. Zhang, 2001, Journal of molecular biology.

Locating a local symmetry axis from patterson map cross vectors: application to crystal data from GroEl, GTP cyclohydrolase I and the proteosome.

R Huber, L A Svensson, M T Stubbs, 1996, Acta crystallographica. Section D, Biological crystallography.

The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.

A Wendel, R. Ladenstein, O. Epp, 1983, European journal of biochemistry.

Proteins from thermophilic and mesophilic organisms essentially do not differ in packing.

A. Karshikoff, R. Ladenstein, A. Karshikoff, 1998, Protein engineering.

Three-dimensional structure of class pi glutathione S-transferase from human placenta in complex with S-hexylglutathione at 2.8 A resolution.

M W Parker, R. Huber, P. Reinemer, 1992, Journal of molecular biology.

Refined crystal structure of ascorbate oxidase at 1.9 A resolution.

L Avigliano, M Bolognesi, R. Huber, 1992, Journal of molecular biology.