Experimental determination of the radiation dose limit for cryocooled protein crystals. - Wikidata - wikimedia - TriplyDB

Experimental determination of the radiation dose limit for cryocooled protein crystals.

Experimental determination of the radiation dose limit for cryocooled protein crystals.

http://www.wikidata.org/entity/Q34596657

about

Serial femtosecond crystallography: the first five years Membrane protein structure determination - the next generation Opportunities and challenges for time-resolved studies of protein structural dynamics at X-ray free-electron lasers.Identifying and quantifying radiation damage at the atomic level In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures.Serial crystallography captures enzyme catalysis in copper nitrite reductase at atomic resolution from one crystal Lipidic cubic phase injector is a viable crystal delivery system for time-resolved serial crystallography Structure and quantum chemical characterization of chloroperoxidase compound 0, a common reaction intermediate of diverse heme enzymes Femtosecond X-ray protein nanocrystallography In vivo protein crystallization opens new routes in structural biology High-Resolution Protein Structure Determination by Serial Femtosecond Crystallography Structure of a photosynthetic reaction centre determined by serial femtosecond crystallography Goniometer-based femtosecond crystallography with X-ray free electron lasers.Shoot-and-Trap: Use of specific x-ray damage to study structural protein dynamics by temperature-controlled cryo-crystallography Crystallographic and Single-Crystal Spectral Analysis of the Peroxidase Ferryl Intermediate Effective scavenging at cryotemperatures: further increasing the dose tolerance of protein crystals Spatial distribution of radiation damage to crystalline proteins at 25–300 K Radiation damage reveals promising interaction position Can radiation damage to protein crystals be reduced using small-molecule compounds?Room temperature femtosecond X-ray diffraction of photosystem II microcrystals Insights into the mechanism of X-ray-induced disulfide-bond cleavage in lysozyme crystals based on EPR, optical absorption and X-ray diffraction studies Structure of -galactosidase at 3.2-A resolution obtained by cryo-electron microscopy Room-temperature macromolecular serial crystallography using synchrotron radiation Structural characterization of nitrosomonas europaea cytochrome c-552 variants with marked differences in electronic structure De novo protein crystal structure determination from X-ray free-electron laser data Crystallographic studies evidencing the high energy tolerance to disrupting the interface disulfide bond of thioredoxin 1 from white leg shrimp Litopenaeus vannamei X-ray diffraction in temporally and spatially resolved biomolecular science X-ray radiation induces deprotonation of the bilin chromophore in crystalline D. radiodurans phytochrome Superoxide reductase from Giardia intestinalis: structural characterization of the first SOR from a eukaryotic organism shows an iron centre that is highly sensitive to photoreduction Radiation damage and derivatization in macromolecular crystallography: a structure factor's perspective RNA protects a nucleoprotein complex against radiation damage Integral membrane proteins and free electron lasers - a compatible couple indeed!EIGER detector: application in macromolecular crystallography High Resolution Structures of Periplasmic Glucose-binding Protein of Pseudomonas putida CSV86 Reveal Structural Basis of Its Substrate Specificity In-vacuum long-wavelength macromolecular crystallography Serial femtosecond crystallography: A revolution in structural biology.Possibilities for serial femtosecond crystallography sample delivery at future light sources.A multicrystal diffraction data-collection approach for studying structural dynamics with millisecond temporal resolution Raster-scanning serial protein crystallography using micro- and nano-focused synchrotron beams A simple technique to reduce evaporation of crystallization droplets by using plate lids with apertures for adding liquids

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P2860

Experimental determination of the radiation dose limit for cryocooled protein crystals.

http://www.wikidata.org/entity/Q34596657

description

2006 nî lūn-bûn

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2006 թուականի Մարտին հրատարակուած գիտական յօդուած

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2006 թվականի մարտին հրատարակված գիտական հոդված

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2006年の論文

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年学术文章

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2006年學術文章

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name

Experimental determination of the radiation dose limit for cryocooled protein crystals.

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Experimental determination of the radiation dose limit for cryocooled protein crystals.

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Experimental determination of the radiation dose limit for cryocooled protein crystals.

@nl

type

label

Experimental determination of the radiation dose limit for cryocooled protein crystals.

@ast

Experimental determination of the radiation dose limit for cryocooled protein crystals.

@en

Experimental determination of the radiation dose limit for cryocooled protein crystals.

@nl

prefLabel

Experimental determination of the radiation dose limit for cryocooled protein crystals.

@ast

Experimental determination of the radiation dose limit for cryocooled protein crystals.

@en

Experimental determination of the radiation dose limit for cryocooled protein crystals.

@nl

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PNAS.0600973103

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

P1476

Experimental determination of the radiation dose limit for cryocooled protein crystals.

@en

P2093

Elspeth F Garman

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Enrique Rudiño-Piñera

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Robin Leslie Owen

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P2860

Specific chemical and structural damage to proteins produced by synchrotron radiation

Structural changes in a cryo-cooled protein crystal owing to radiation damage

Atomic resolution structures of trypsin provide insight into structural radiation damage

Specific radiation damage can be used to solve macromolecular crystal structures

Coot: model-building tools for molecular graphics

REFMAC5 dictionary: organization of prior chemical knowledge and guidelines for its use

Integration of macromolecular diffraction data

Improved R-factors for diffraction data analysis in macromolecular crystallography

When X-rays modify the protein structure: radiation damage at work.

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

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