Analysis of Global and Site-Specific Radiation Damage in Cryo-EM (Q58037985)

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title

Analysis of Global and Site-Specific Radiation Damage in Cryo-EM (English)

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25 March 2020

Marcus Gallagher-Jones

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author name string

Dan Shi

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Calina Glynn

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Chih-Te Zee

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Michael W Martynowycz

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Jose A Rodriguez

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Tamir Gonen

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publication date

26 April 2018

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volume

26

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issue

5

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page(s)

759-766.e4

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Radiation damage of purple membrane at low temperature

25 March 2020

cites work

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12 December 2020

Three-dimensional model of purple membrane obtained by electron microscopy

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Quantitative assessment of radiation damage in a thin protein crystal

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The potential and limitations of neutrons, electrons and X-rays for atomic resolution microscopy of unstained biological molecules

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Specific chemical and structural damage to proteins produced by synchrotron radiation

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Investigation of possible free-radical scavengers and metrics for radiation damage in protein cryocrystallography

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Unit-cell volume change as a metric of radiation damage in crystals of macromolecules

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Will reduced radiation damage occur with very small crystals?

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12 December 2020

Some aspects of quantitative analysis and correction of radiation damage

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Quantifying X-ray radiation damage in protein crystals at cryogenic temperatures

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A short history of SHELX

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12 December 2020

A beginner's guide to radiation damage

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The resolution dependence of optimal exposures in liquid nitrogen temperature electron cryomicroscopy of catalase crystals.

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Integration, scaling, space-group assignment and post-refinement

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12 December 2020

Radiation damage in macromolecular crystallography: what is it and why should we care?

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12 December 2020

An assessment of the resolution limitation due to radiation-damage in x-ray diffraction microscopy

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12 December 2020

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

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Overview of the CCP4 suite and current developments

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12 December 2020

iMOSFLM: a new graphical interface for diffraction-image processing with MOSFLM

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12 December 2020

REFMAC5 for the refinement of macromolecular crystal structures

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12 December 2020

Global radiation damage: temperature dependence, time dependence and how to outrun it.

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How good are my data and what is the resolution?

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12 December 2020

On effective and optical resolutions of diffraction data sets

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Three-dimensional electron crystallography of protein microcrystals

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Structure of -galactosidase at 3.2-A resolution obtained by cryo-electron microscopy

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High-resolution structure determination by continuous-rotation data collection in MicroED.

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12 December 2020

Structure of catalase determined by MicroED

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Radiation damage to nucleoprotein complexes in macromolecular crystallography.

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Radiation decay of thaumatin crystals at three X-ray energies

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12 December 2020

Serial femtosecond crystallography: the first five years

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12 December 2020

Measuring the optimal exposure for single particle cryo-EM using a 2.6 Å reconstruction of rotavirus VP6

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12 December 2020

MicroED data collection and processing.

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12 December 2020

EMRinger: side chain-directed model and map validation for 3D cryo-electron microscopy.

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12 December 2020

The collection of MicroED data for macromolecular crystallography

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12 December 2020

Breaking Cryo-EM Resolution Barriers to Facilitate Drug Discovery.

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12 December 2020

Modeling truncated pixel values of faint reflections in MicroED images

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12 December 2020

Atomic-resolution structures from fragmented protein crystals with the cryoEM method MicroED.

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12 December 2020

10.1016/J.STR.2018.03.021

Identifiers

DOI

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25 March 2020

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PubMed publication ID

29706530

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