R
Rudolf Ladenstein
Researcher at Karolinska Institutet
Publications - 141
Citations - 8616
Rudolf Ladenstein is an academic researcher from Karolinska Institutet. The author has contributed to research in topics: Lumazine synthase & Riboflavin synthase. The author has an hindex of 48, co-authored 141 publications receiving 8213 citations. Previous affiliations of Rudolf Ladenstein include Max Planck Society & Bulgarian Academy of Sciences.
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Journal ArticleDOI
The refined structure of the selenoenzyme glutathione peroxidase at 0.2-nm resolution.
TL;DR: A general picture of a minimal reaction mechanism, in good agreement with functional and structural data, is proposed and a reasonable model of glutathione binding is presented.
Journal ArticleDOI
Critical Residues for Structure and Catalysis in Short-chain Dehydrogenases/Reductases
Charlotta Filling,Kurt D. Berndt,Kurt D. Berndt,Jordi Benach,Stefan Knapp,Tim Prozorovski,Erik Nordling,Rudolf Ladenstein,Hans Jörnvall,Udo Oppermann +9 more
TL;DR: This work has analyzed the role of several conserved residues regarding folding, stability, steady-state kinetics, and coenzyme binding using bacterial 3β/17β-hydroxysteroid dehydrogenase and selected mutants to form a tetrad of Asn-Ser-Tyr-Lys in the majority of characterized short-chain dehydrogenases/reductase enzymes.
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Refined crystal structure of ascorbate oxidase at 1.9 A resolution.
Albrecht Messerschmidt,Rudolf Ladenstein,Robert Huber,Martino Bolognesi,Luciana Avigliano,Raffaele Petruzzelli,Antonello Rossi,Alessandro Finazzi-Agrò +7 more
TL;DR: The crystal structure of the fully oxidized form of ascorbate oxidase from Zucchini has been refined at 1.90 A (1 A = 0.1 nm) resolution, using an energy-restrained least-squares refinement procedure.
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X-ray crystal structure of the blue oxidase ascorbate oxidase from zucchini. Analysis of the polypeptide fold and a model of the copper sites and ligands.
Albrecht Messerschmidt,Antonello Rossi,Rudolf Ladenstein,Robert Huber,Martino Bolognesi,Guiseppina Gatti,Augusto Marchesini,Raffaele Petruzzelli,Alessandro Finazzi-Agrò +8 more
TL;DR: Two crystal forms of the multi-copper protein ascorbate oxidase from Zucchini have been analysed at 2.5 A resolution and a model of the polypeptide chain and the copper ions and their ligands has been built.
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The three-dimensional structure of class pi glutathione S-transferase in complex with glutathione sulfonate at 2.3 A resolution.
TL;DR: The three‐dimensional structure of class pi glutathione S‐transferase from pig lung, a homodimeric enzyme, has been solved by multiple isomorphous replacement at 3 A resolution and preliminarily refined at 2.3 A resolution.