In situ serial crystallography for rapid de novo membrane protein structure determination

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: Online-Ressource

Language: Englisch

Bibliographic citation: In: Communications Biology ; 1 (2018). - 124. - eISSN 2399-3642

Classification: Biowissenschaften, Biologie

Event: Veröffentlichung

(where): Konstanz

(who): Bibliothek der Universität Konstanz

(when): 2018

Creator: Huang, Chia-Ying
Olieric, Vincent
Howe, Nicole
Warshamanage, Rangana
Weinert, Tobias
Panepucci, Ezequiel
Vogeley, Lutz
Diederichs, Kay
Caffrey, Martin
Wang, Meitian

URN: urn:nbn:de:bsz:352-2-mg91oyv9c3g53

Rights: Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 25.03.2025, 1:57 PM CET

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Associated

Huang, Chia-Ying
Olieric, Vincent
Howe, Nicole
Warshamanage, Rangana
Weinert, Tobias
Panepucci, Ezequiel
Vogeley, Lutz
Diederichs, Kay
Caffrey, Martin
Wang, Meitian
Bibliothek der Universität Konstanz

Time of origin

2018

Other Objects (12)

Breaking the indexing ambiguity in serial crystallography

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Structure of the outer membrane protein FhuA presents a binding mode for Lipopolysaccharide

$Improved R-factors for diffraction data analysis in macromolecular crystallography$

Improved R-factors for diffraction data analysis in macromolecular crystallography

In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures

$Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein$

Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein

Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach

Dissecting random and systematic differences between noisy composite data sets

Quantifying instrument errors in macromolecular X-ray data sets

Breaking the indexing ambiguity in serial crystallography

Identification of rogue datasets in serial crystallography

Computing in macromolecular crystallography using a parallel architecture

In meso in situ serial X-ray crystallography of soluble and membrane proteins

Assessing and maximizing data quality in macromolecular crystallography

Structure of the outer membrane protein FhuA presents a binding mode for Lipopolysaccharide

$Improved R-factors for diffraction data analysis in macromolecular crystallography$

Improved R-factors for diffraction data analysis in macromolecular crystallography

In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures

$Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein$

Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein

Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach

Dissecting random and systematic differences between noisy composite data sets

Quantifying instrument errors in macromolecular X-ray data sets

Breaking the indexing ambiguity in serial crystallography

Identification of rogue datasets in serial crystallography

Computing in macromolecular crystallography using a parallel architecture

In meso in situ serial X-ray crystallography of soluble and membrane proteins

Assessing and maximizing data quality in macromolecular crystallography

Structure of the outer membrane protein FhuA presents a binding mode for Lipopolysaccharide

$Improved R-factors for diffraction data analysis in macromolecular crystallography$

Improved R-factors for diffraction data analysis in macromolecular crystallography

In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures

$Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein$

Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein

Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach

Dissecting random and systematic differences between noisy composite data sets

Quantifying instrument errors in macromolecular X-ray data sets

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In situ serial crystallography for rapid de novo membrane protein structure determination

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Other Objects (12)

Breaking the indexing ambiguity in serial crystallography

Identification of rogue datasets in serial crystallography

Computing in macromolecular crystallography using a parallel architecture

In meso in situ serial X-ray crystallography of soluble and membrane proteins

Assessing and maximizing data quality in macromolecular crystallography

Structure of the outer membrane protein FhuA presents a binding mode for Lipopolysaccharide

Improved R-factors for diffraction data analysis in macromolecular crystallography

In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures

Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein

Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach

Dissecting random and systematic differences between noisy composite data sets

Quantifying instrument errors in macromolecular X-ray data sets

Breaking the indexing ambiguity in serial crystallography

Identification of rogue datasets in serial crystallography

Computing in macromolecular crystallography using a parallel architecture

In meso in situ serial X-ray crystallography of soluble and membrane proteins

Assessing and maximizing data quality in macromolecular crystallography

Structure of the outer membrane protein FhuA presents a binding mode for Lipopolysaccharide

Improved R-factors for diffraction data analysis in macromolecular crystallography

In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures

Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein

Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach

Dissecting random and systematic differences between noisy composite data sets

Quantifying instrument errors in macromolecular X-ray data sets

Breaking the indexing ambiguity in serial crystallography

Identification of rogue datasets in serial crystallography

Computing in macromolecular crystallography using a parallel architecture

In meso in situ serial X-ray crystallography of soluble and membrane proteins

Assessing and maximizing data quality in macromolecular crystallography

Structure of the outer membrane protein FhuA presents a binding mode for Lipopolysaccharide

Improved R-factors for diffraction data analysis in macromolecular crystallography

In meso in situ serial X-ray crystallography of soluble and membrane proteins at cryogenic temperatures

Purification, crystallization and preliminary diffraction studies of AcrB, an inner-membrane multi-drug efflux protein

Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach

Dissecting random and systematic differences between noisy composite data sets

Quantifying instrument errors in macromolecular X-ray data sets

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