Journal ArticleDOI
CRYSOL : a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
TLDR
In this paper, a program for evaluating the solution scattering from macromolecules with known atomic structure is presented, which uses multipole expansion for fast calculation of the spherically averaged scattering pattern and takes into account the hydration shell.Abstract:
A program for evaluating the solution scattering from macromolecules with known atomic structure is presented. The program uses multipole expansion for fast calculation of the spherically averaged scattering pattern and takes into account the hydration shell. Given the atomic coordinates (e.g. from the Brookhaven Protein Data Bank) it can either predict the solution scattering curve or fit the experimental scattering curve using only two free parameters, the average displaced solvent volume per atomic group and the contrast of the hydration layer. The program runs on IBM PCs and on the major UNIX platforms.read more
Citations
More filters
Journal ArticleDOI
The structure of (CENP-A–H4) 2 reveals physical features that mark centromeres
TL;DR: DNA topological analysis indicates that CENP-A-containing nucleosomes are octameric with conventional left-handed DNA wrapping, in contrast to other recent proposals, indicating specificity for an unconventional nucleosome shape.
Journal ArticleDOI
Refinement of multidomain protein structures by combination of solution small-angle X-ray scattering and NMR data.
TL;DR: A computational procedure is described that allows incorporation of experimental information from small-angle scattering of X-ray radiation in solution (SAXS) data into the mainstream high-resolution macromolecular structure refinement and is expected to become useful for multidomain proteins, multimeric assemblies, and tight macromolescular complexes.
Journal ArticleDOI
The lattice as allosteric effector: Structural studies of αβ- and γ-tubulin clarify the role of GTP in microtubule assembly
TL;DR: Results support the lattice model by demonstrating that major domain rearrangements do not occur in eukaryotic tubulins in response to GTP binding, and that the unpolymerized conformation of αβ-tubulin differs significantly from the polymerized one.
Journal ArticleDOI
Structural basis of hepatocyte growth factor/scatter factor and MET signalling.
Ermanno Gherardi,Sara Sandin,Maxim V. Petoukhov,John T. Finch,Mark Youles,Lars-Göran Öfverstedt,Ricardo Núñez Miguel,Tom L. Blundell,George F. Vande Woude,Ulf Skoglund,Dmitri I. Svergun +10 more
TL;DR: The study shows how the proteolytic mechanism of activation of the complex proteinases has been adapted to cell signaling in vertebrate organisms, offers a description of monomeric and dimeric ligand-receptor complexes, and provides a foundation to the structural basis of HGF/SF-MET signaling.
Journal ArticleDOI
Sequence Determinants of the Conformational Properties of an Intrinsically Disordered Protein Prior to and upon Multisite Phosphorylation
TL;DR: It is shown that the unphosphorylated Ash1 IDR adopts coil-like conformations that are expanded and well-solvated, and this result contradicts inferences regarding global compaction that are derived from heuristics based on amino acid compositions for IDRs with low proline contents.
References
More filters
Book
International tables for X-ray crystallography
Norman Fordyce McKerron Henry,Lonsdale, Kathleen, Dame,John S. Kasper,Caroline H. MacGillavry,Gerard D. Rieck,James A. Ibers,Walter C. Hamilton +6 more
Angular Momentum in Quantum Mechanics
TL;DR: In this paper, the angular momentum, one of the most fundamental quantities in all of quantum mechanics, is introduced and a concise introduction to its application in atomic, molecular, and nuclear physics is provided.
Book
Angular Momentum in Quantum Mechanics
TL;DR: In this article, the angular momentum, one of the most fundamental quantities in all of quantum mechanics, is introduced and a concise introduction to its application in atomic, molecular, and nuclear physics is provided.