Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL - Test2 - elhamkhani - TriplyDB

Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL

Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL

http://www.wikidata.org/entity/Q27690173

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Challenging Density Functional Theory Calculations with Hemes and Porphyrins Sub-atomic resolution X-ray crystallography and neutron crystallography: promise, challenges and potential Serial femtosecond crystallography: the first five years Acoustic Injectors for Drop-On-Demand Serial Femtosecond Crystallography.Automated harvesting and processing of protein crystals through laser photoablation A modular and compact portable mini-endstation for high-precision, high-speed fixed target serial crystallography at FEL and synchrotron sources.Single Enzyme Experiments Reveal a Long-Lifetime Proton Leak State in a Heme-Copper Oxidase Goniometer-based femtosecond crystallography with X-ray free electron lasers.Native structure of photosystem II at 1.95 Å resolution viewed by femtosecond X-ray pulses Room-temperature serial crystallography at synchrotron X-ray sources using slowly flowing free-standing high-viscosity microstreams Fixed target combined with spectral mapping: approaching 100% hit rates for serial crystallography Advances in X-ray free electron laser (XFEL) diffraction data processing applied to the crystal structure of the synaptotagmin-1 / SNARE complex Integrative, dynamic structural biology at atomic resolution--it's about time Cardiolipin Interactions with Proteins Protein Crystallography from the Perspective of Technology Developments XFELs open a new era in structural chemical biology Metalloprotein structures at ambient conditions and in real-time: biological crystallography and spectroscopy using X-ray free electron lasers Serial femtosecond crystallography: A revolution in structural biology.Protein structure determination by single-wavelength anomalous diffraction phasing of X-ray free-electron laser data.Possibilities for serial femtosecond crystallography sample delivery at future light sources.Capture and X-ray diffraction studies of protein microcrystals in a microfluidic trap array.Data Exploration Toolkit for serial diffraction experiments.Current advances in synchrotron radiation instrumentation for MX experiments Fixed-target protein serial microcrystallography with an x-ray free electron laser.In situ serial Laue diffraction on a microfluidic crystallization device Proton translocation in cytochrome c oxidase: insights from proton exchange kinetics and vibrational spectroscopy.Enabling X-ray free electron laser crystallography for challenging biological systems from a limited number of crystals.Overview of the SACLA facility.Radiation damage to macromolecules: kill or cure?Indications of radiation damage in ferredoxin microcrystals using high-intensity X-FEL beams.Coherent X-Ray Diffraction Imaging of Chloroplasts from Cyanidioschyzon merolae by Using X-Ray Free Electron Laser.The potential of future light sources to explore the structure and function of matter Mapping the conformational landscape of a dynamic enzyme by multitemperature and XFEL crystallography.A high-transparency, micro-patternable chip for X-ray diffraction analysis of microcrystals under native growth conditions Towards time-resolved serial crystallography in a microfluidic device.Goniometer-based femtosecond X-ray diffraction of mutant 30S ribosomal subunit crystals.Time-resolved structural studies with serial crystallography: A new light on retinal proteins.Cryogenic coherent X-ray diffraction imaging of biological samples at SACLA: a correlative approach with cryo-electron and light microscopy.A beam branching method for timing and spectral characterization of hard X-ray free-electron lasers TAKASAGO-6 apparatus for cryogenic coherent X-ray diffraction imaging of biological non-crystalline particles using X-ray free electron laser at SACLA.

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P2860

Determination of damage-free crystal structure of an X-ray-sensitive protein using an XFEL

http://www.wikidata.org/entity/Q27690173

description

2014 nî lūn-bûn

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2014 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի հուլիսին հրատարակված գիտական հոդված

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2014年の論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年論文

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2014年论文

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name

Determination of damage-free c ...... ensitive protein using an XFEL

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Determination of damage-free c ...... ensitive protein using an XFEL

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Determination of damage-free c ...... ensitive protein using an XFEL

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Determination of damage-free c ...... ensitive protein using an XFEL

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Determination of damage-free c ...... ensitive protein using an XFEL

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Determination of damage-free c ...... ensitive protein using an XFEL

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Determination of damage-free c ...... ensitive protein using an XFEL

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Determination of damage-free c ...... ensitive protein using an XFEL

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Determination of damage-free c ...... ensitive protein using an XFEL

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Determination of damage-free c ...... ensitive protein using an XFEL

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Go Ueno

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Hideo Ago

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Hironori Murakami

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Hiroshi Sugimoto

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Jian-Ren Shen

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

Kazumasa Muramoto

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

Kensuke Tono

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

Kyoko Shinzawa-Itoh

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

Miki Hatanaka

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

Naomine Yano

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

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PHENIX: a comprehensive Python-based system for macromolecular structure solution

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734-6

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scholarly article

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2426438

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10.1038/NMETH.2962

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7

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11

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Masaki Yamamoto

Tetsuya Ishikawa

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2014-07-01T00:00:00Z

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1027112154

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24813624

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protein structure

X-ray crystallography

crystal structure