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Miroslawa Dauter

Researcher at Argonne National Laboratory

Publications -  31
Citations -  859

Miroslawa Dauter is an academic researcher from Argonne National Laboratory. The author has contributed to research in topics: Protein structure & Crystal structure. The author has an hindex of 17, co-authored 31 publications receiving 780 citations. Previous affiliations of Miroslawa Dauter include Polish Academy of Sciences & University of York.

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Triclinic Lysozyme at 0.65 A Resolution.

TL;DR: The crystal structure of triclinic hen egg-white lysozyme (HEWL) has been refined against diffraction data extending to 0.65 A resolution measured at 100 K using synchrotron radiation, and the occupancies of the water sites were refined.
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Structural basis of interactions between human glutamate carboxypeptidase II and its substrate analogs

TL;DR: The S1 pocket of GCPII could be accurately defined and analyzed for the first time, and the data indicate the importance of Asn519, Arg463, Arg534, and Arg536 for recognition of the penultimate substrate residues, as well as mechanistic explanation of G CPII preference for acidic dipeptides.
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Structure and function of Humicola insolens family 6 cellulases: structure of the endoglucanase, Cel6B, at 1.6 A resolution.

TL;DR: The structure of the catalytic core of the family 6 endoglucanase Cel6B from Humicola insolens has been solved by molecular replacement with the known T. reesei cellobiohydrolase II as the search model and reveals that the deletion of just a single loop of the active site peels open the active-site tunnel to reveal a substrate-binding groove.
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On the reproducibility of protein crystal structures: five atomic resolution structures of trypsin.

TL;DR: Many details of a protein structure are reproducible or to what extent they might differ in models obtained from different crystals, however, several features of residues or ligands located in flexible parts of the macromolecule may vary significantly, such as side-chain orientations and the occupancies of certain fragments.
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High regularity of Z-DNA revealed by ultra high-resolution crystal structure at 0.55 Å

TL;DR: Comparisons of the stereochemical library values with the present accurate Z-DNA parameters, shows in general a good agreement, but also reveals significant discrepancies in the description of guanine-sugar valence angles and in the geometry of the phosphate groups.