Zobrazeno 1 - 10
of 99
pro vyhledávání: '"Donald L. D. Caspar"'
Autor:
Donald L. D. Caspar, Alexei S. Soares
Publikováno v:
Journal of Structural Biology. 200:213-218
X-ray crystallographic measurement of the number of solvent electrons in the unit cell of a protein crystal equilibrated with aqueous solutions of different densities provides information about preferential hydration in the crystalline state. Room te
Autor:
Toshihiro Omura, R. Holland Cheng, Donald L. D. Caspar, Yoshinori Fujiyoshi, Keiichi Namba, Naoyuki Miyazaki, Fredrik Sjöborg, Koji Yonekura, Kazuyoshi Murata, Bomu Wu, Lena Marmstål Hammar, Kenji Iwasaki, Yafeng Zhu
Publikováno v:
Journal of Molecular Biology. 383:252-265
In the double-shelled capsid of Phytoreovirus, the outer capsid attaches firmly to the 3-fold axes of the T=1 core. It then forms a T=13 lattice via lateral interactions among the P8 trimers (Wu et al., 2000, Virology 271, 18-25). Purified P8 molecul
Publikováno v:
Journal of Molecular Biology. 346:307-318
The structural and energetic consequences of modifications to the hydrophobic cavity of interleukin 1-beta (IL-1beta) are described. Previous reports demonstrated that the entirely hydrophobic cavity of IL-1beta contains positionally disordered water
Autor:
Johannes Zellner, Kerstin Hölzer, Klaus Schroer, Edgar Weckert, Annie Heroux, Robert M. Sweet, Alexei S. Soares, William Nolan, Dieter K. Schneider, Donald L. D. Caspar
Publikováno v:
Acta Crystallographica Section D Biological Crystallography. 59:1716-1724
Triplet phases recorded from insulin crystals were used to measure the improvement of phases during model refinement and to quantify the contribution made by each step in the refinement. Conventional amplitude data were recorded to 1.5 A resolution f
Autor:
Chris Long, Melinda Balbirnie, Donald L. D. Caspar, Ruben Diaz-Avalos, David Eisenberg, Robert Grothe, Eric Fontano
Publikováno v:
Journal of Molecular Biology. 330:1165-1175
The seven-residue peptide GNNQQNY from the N-terminal region of the yeast prion protein Sup35, which forms amyloid fibers, colloidal aggregates and highly ordered nanocrystals, provides a model system for characterizing the elusively protean cross-be
Publikováno v:
Proceedings of the National Academy of Sciences. 98:11259-11264
Understanding how metal binding regulates the activity of the diphtheria toxin repressor protein (DtxR) requires information about the structure in solution. We have prepared a DtxR mutant construct with three additional N-terminal residues, Gly-Ser-
Publikováno v:
Biophysical Journal. 74(1):604-615
Previous x-ray studies (2.8-Å resolution) on crystals of tobacco mosaic virus coat protein grown from solutions containing high salt have characterized the structure of the protein aggregate as a dimer of a bilayered cylindrical disk formed by 34 ch
Autor:
Ruben Diaz-Avalos, Donald L. D. Caspar
Publikováno v:
Biophysical Journal. 74:595-603
The coat protein of tobacco mosaic virus is known to form three different classes of aggregate, depending on environmental conditions, namely helical, disk, and A-protein. Among the disk aggregates, there are four-layer, six-layer, and long stacks, w
Publikováno v:
Ultramicroscopy. 55:383-395
The development of low-dose electron cryo-microscopy has provided the means to see structural details to better than 10 A resolution in helical structures. The application of techniques of image analysis to micrographs can yield accurate phases, but
Publikováno v:
Proceedings of the National Academy of Sciences. 91:1224-1228
To determine the distribution of monovalent cations around a protein we have measured anomalous scattering diffraction data from Tl-containing cubic insulin crystals at pH 8 and pH 10.5. The differences between Bijvoet reflection pairs within each se