Radiation damage in protein crystals is reduced with a micron-sized X-ray beam. - Wikidata - awgldk - TriplyDB

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

http://www.wikidata.org/entity/Q34794647

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Acoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography.In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures.Quaternary ammonium oxidative demethylation: X-ray crystallographic, resonance Raman, and UV-visible spectroscopic analysis of a Rieske-type demethylase Room-temperature macromolecular serial crystallography using synchrotron radiation Mitigation of X-ray damage in macromolecular crystallography by submicrometre line focusing Nonlinear Optical Characterization of Membrane Protein Microcrystals and Nanocrystals.Acoustic methods for high-throughput protein crystal mounting at next-generation macromolecular crystallographic beamlines.On the variability of experimental data in macromolecular crystallography An X-ray transparent microfluidic platform for screening of the phase behavior of lipidic mesophases.Developments in optics and performance at BL13-XALOC, the macromolecular crystallography beamline at the ALBA synchrotron.In meso in situ serial X-ray crystallography of soluble and membrane proteins Dark progression reveals slow timescales for radiation damage between T = 180 and 240 K.Micro-crystallography comes of age.Predicted optical performance of the GM/CA@APS micro-focus beamline Kinetic modeling of the X-ray-induced damage to a metalloprotein.Macromolecular crystallography radiation damage research: what's new?Imaging local electric fields produced upon synchrotron X-ray exposure Automated sample-scanning methods for radiation damage mitigation and diffraction-based centering of macromolecular crystals.Radiation damage to macromolecules: kill or cure?Fast fluorescence techniques for crystallography beamlines.Global radiation damage at 300 and 260 K with dose rates approaching 1 MGy s⁻¹.A high-transparency, micro-patternable chip for X-ray diffraction analysis of microcrystals under native growth conditions Radiation damage in a micron-sized protein crystal studied via reciprocal space mapping and Bragg coherent diffractive imaging.Guiding synchrotron X-ray diffraction by multimodal video-rate protein crystal imaging.Locating and Visualizing Crystals for X-Ray Diffraction Experiments.Applications of X-Ray Micro-Beam for Data Collection.Radiation Damage in Macromolecular Crystallography.Global radiation damage: temperature dependence, time dependence and how to outrun it.Identification of patterns in diffraction intensities affected by radiation exposure Quantifying radiation damage in biomolecular small-angle X-ray scattering.Bragg coherent diffraction imaging and metrics for radiation damage in protein micro-crystallography Crystal structure of CO-bound cytochrome c oxidase determined by serial femtosecond X-ray crystallography at room temperature.Dynamic X-ray diffraction sampling for protein crystal positioning.Radiation damage to nucleoprotein complexes in macromolecular crystallography.A survey of global radiation damage to 15 different protein crystal types at room temperature: a new decay model.Protein microcrystallography using synchrotron radiation.Diffraction-limited storage rings - a window to the science of tomorrow.Lifetimes and spatio-temporal response of protein crystals in intense X-ray microbeams.Estimate your dose: RADDOSE-3D.Optimizing the spatial distribution of dose in X-ray macromolecular crystallography.

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P2860

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

http://www.wikidata.org/entity/Q34794647

description

2011 nî lūn-bûn

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2011 թուականի Մարտին հրատարակուած գիտական յօդուած

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2011 թվականի մարտին հրատարակված գիտական հոդված

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2011年の論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年論文

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2011年论文

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name

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

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Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

@en

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

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type

label

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

@ast

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

@en

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

@nl

prefLabel

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

@ast

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

@en

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

@nl

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PNAS.1017701108

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Proceedings of the National Academy of Sciences of the United States of America

P1476

Radiation damage in protein crystals is reduced with a micron-sized X-ray beam.

@en

P2093

Derek W Yoder

http://www.w3.org/2001/XMLSchema#string

Gerd Rosenbaum

http://www.w3.org/2001/XMLSchema#string

Janet L Smith

http://www.w3.org/2001/XMLSchema#string

Oleg A Makarov

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Richard Benn

http://www.w3.org/2001/XMLSchema#string

Robert F Fischetti

http://www.w3.org/2001/XMLSchema#string

Ruslan Sanishvili

http://www.w3.org/2001/XMLSchema#string

Sergey Stepanov

http://www.w3.org/2001/XMLSchema#string

Shenglan Xu

http://www.w3.org/2001/XMLSchema#string

Stephen Corcoran

http://www.w3.org/2001/XMLSchema#string

P2860

Structure of the cross-beta spine of amyloid-like fibrils

Specific radiation damage can be used to solve macromolecular crystal structures

Crystal structure of the human beta2 adrenergic G-protein-coupled receptor

Protein crystallography with a micrometre-sized synchrotron-radiation beam

Zero-dose extrapolation as part of macromolecular synchrotron data reduction.

Observation of time-resolved structural changes by linear interpolation of highly redundant X-ray diffraction data.

A 7μm mini-beam improves diffraction data from small or imperfect crystals of macromolecules

The optimum conditions to collect X-ray data from very small samples.

The minimum crystal size needed for a complete diffraction data set.

Know your dose: RADDOSE

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6127-6132

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scholarly article

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10.1073/PNAS.1017701108

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15

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108

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2011-03-28T00:00:00Z

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50891853

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21444772

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X-ray crystallography

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3076849

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