Zbyszek Otwinowski
University of Texas Southwestern Medical Center
127 Papers
575 Citations
Zbyszek Otwinowski is an academic researcher from University of Texas Southwestern Medical Center. The author has contributed to research in topics: Biology & Protein structure. The author has an hindex of 43, co-authored 115 publications. Previous affiliations of Zbyszek Otwinowski include University of Illinois at Chicago & University of Texas at Dallas.
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Papers
Crystallization and preliminary X-ray diffraction analysis of Val57 mutants of the amyloidogenic protein human cystatin C
Marta Orlikowska,Elżbieta Jankowska,Dominika Borek,Zbyszek Otwinowski,Piotr M. Skowron,Aneta Szymańska +5 more
TL;DR: To assess the influence of changes in the sequence and properties of loop L1 on the dimerization propensity of cystatin C, two additional hCC mutants were obtained: one with a residue favoured in β-turns and another with proline, a residue that is known to be a structural element that can rigidify but also broaden turns.
The crystallographic fast Fourier transform. III. Centred lattices.
TL;DR: Algorithms for evaluation of the crystallographic FFT for centred lattices are presented and, for 44 groups, combining these algorithms with those described by Rowicka, Kudlicki & Otwinowski yields the maximal symmetry reduction.
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The His-tag as a decoy modulating preferred orientation in cryoEM
Raquel Bromberg,Yirui Guo,Daniel A. Plymire,Tabitha Emde,Maciej Puzio,Dominika Borek,Zbyszek Otwinowski +6 more
TL;DR: It is shown here that His-tag presence affects how coproheme decarboxylase interacts with the water-air interface during grid preparation for cryoEM, and thus may be used to modulate these interactions, including inducing changes in patterns of preferred orientation.
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Application of Maximum Entropy principle to modeling torsion angle probability distribution in proteins
Małgorzata Rowicka,Zbyszek Otwinowski +1 more
- 08 Jun 2004
TL;DR: Using the Maximum Entropy principle, a probability distribution of torsion angles in proteins is found by implementing the conjugate gradient method in Polak‐Ribiere variant and practical approximations of the theoretical distribution are investigated.
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Monomer and dimer structures of cytochrome bo3 ubiquinol oxidase from Escherichia coli
TL;DR: In this article , the E. coli cytochrome bo3 ubiquinol oxidase was reconstituted in amphipol by cryogenic electron microscopy single particle reconstruction (cryo-EM SPR) to a resolution of 3.15 Å and 3.46 Å, respectively.
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