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Zbigniew Dauter

Researcher at Brookhaven National Laboratory

Publications -  151
Citations -  9775

Zbigniew Dauter is an academic researcher from Brookhaven National Laboratory. The author has contributed to research in topics: Crystal structure & Protein structure. The author has an hindex of 49, co-authored 149 publications receiving 9439 citations. Previous affiliations of Zbigniew Dauter include Brookhaven College & Humboldt University of Berlin.

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Molecular basis of agonism and antagonism in the oestrogen receptor.

TL;DR: The crystal structures of the LBD of ER in complex with the endogenous oestrogen, 17β-oestradiol, and the selective antagonist raloxifene provide a molecular basis for the distinctive pharmacophore of the ER and its catholic binding properties.
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Novel approach to phasing proteins: derivatization by short cryo‐soaking with halides

TL;DR: This approach has been tested successfully on four different proteins and has been used to solve the structure of a new protein of molecular weight 30 kDa.
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Can anomalous signal of sulfur become a tool for solving protein crystal structures

TL;DR: Using solely a native crystal of tetragonal hen egg-white lysozyme, a protein of 14 kDa molecular mass, it was possible to detect the positions of the ten sulfur and seven chlorine atoms from their anomalous signal, and proceed from there to obtain an electron-density map of very high quality.
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Structural basis for Diels-Alder ribozyme-catalyzed carbon-carbon bond formation

TL;DR: In this paper, the crystal structures of a ribozyme that catalyzes enantioselective carbon-carbon bond formation by the Diels-Alder reaction in the unbound state and in complex with a reaction product were reported.
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The Escherichia coli malonyl-CoA:acyl carrier protein transacylase at 1.5-A resolution. Crystal structure of a fatty acid synthase component.

TL;DR: The crystal structure is reported here the crystal structure of the malonyl-CoA specific transferase from Escherichia coli, which has an α/β type architecture, but its fold is unique.