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.
Chat about Author
Papers
Processing of X-ray diffraction data collected in oscillation mode
Zbyszek Otwinowski,Wladek Minor +1 more
TL;DR: The methods presented in the chapter have been applied to solve a large variety of problems, from inorganic molecules with 5 A unit cell to rotavirus of 700 A diameters crystallized in 700 × 1000 × 1400 A cell.
33.6K
HKL-3000: the integration of data reduction and structure solution--from diffraction images to an initial model in minutes.
TL;DR: A new approach that integrates data collection, data reduction, phasing and model building significantly accelerates the process of structure determination and on average minimizes the number of data sets and synchrotron time required for structure solution.
Crystallographic analysis of the interaction of the glucocorticoid receptor with DNA.
B. F. Luisi,W. X. Xu,Zbyszek Otwinowski,Leonard P. Freedman,Leonard P. Freedman,Keith R. Yamamoto,Paul B. Sigler +6 more
TL;DR: Two crystal structures of the glucocorticoid receptor DNA-binding domain complexed with DNA are reported, which have a globular fold which contains two Zn-nucleated substructures of distinct conformation and function.
1.5K
The crystal structure of the bacterial chaperonin GroEL at 2.8 A.
Kerstin Braig,Zbyszek Otwinowski,Zbyszek Otwinowski,Rashmi Hegde,Rashmi Hegde,David C Boisvert,Andrzej Joachimiak,Andrzej Joachimiak,Arthur L. Horwich,Paul B. Sigler +9 more
TL;DR: The crystal structure of Escherichia coli GroEL shows a porous cylinder of 14 subunits made of two nearly 7-fold rotationally symmetrical rings stacked back-to-back with dyad symmetry.
1.3K
Interfacial catalysis: the mechanism of phospholipase A2
TL;DR: Comparison of the cobra-venom complex with the uninhibited PLA2 indicates that optimal binding and catalysis at the lipid-water interface is due to facilitated substrate diffusion from the interfacial binding surface to the catalytic site rather than an allosteric change in the enzyme's structure.