In situ serial crystallography for rapid de novo membrane protein structure determination
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
-
2399-3642
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
-
online resource.
- Bibliographic citation
-
In situ serial crystallography for rapid de novo membrane protein structure determination ; volume:1 ; number:1 ; day:27 ; month:8 ; year:2018 ; pages:1-8 ; date:12.2018
Communications biology ; 1, Heft 1 (27.8.2018), 1-8, 12.2018
- Classification
-
Biowissenschaften, Biologie
- Creator
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Huang, Chia-Ying
- Contributor
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Olieric, Vincent
Howe, Nicole
Warshamanage, Rangana
Weinert, Tobias
Panepucci, Ezequiel
Vogeley, Lutz
Basu, Shibom
Diederichs, Kay
Caffrey, Martin
Wang, Meitian
SpringerLink (Online service)
- DOI
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10.1038/s42003-018-0123-6
- URN
-
urn:nbn:de:101:1-2018092808510249975133
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:38 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Huang, Chia-Ying
- Olieric, Vincent
- Howe, Nicole
- Warshamanage, Rangana
- Weinert, Tobias
- Panepucci, Ezequiel
- Vogeley, Lutz
- Basu, Shibom
- Diederichs, Kay
- Caffrey, Martin
- Wang, Meitian
- SpringerLink (Online service)
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 situ serial crystallography for rapid de novo membrane protein structure determination
Assessing and maximizing data quality 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
Making a difference in multi-data-set crystallography : simple and deterministic data-scaling/selection methods
A comparison of some heavy-atom refinement and phasing programs in a test case
Quantifying instrument errors in macromolecular X-ray data sets
Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach
SUPERIMPOSE - a program for the unambiguous structural superposition of spatially related molecules, including macromolecules
Breaking the indexing ambiguity in serial crystallography
Identification of rogue datasets in serial crystallography
Computing in macromolecular crystallography using a parallel architecture
In situ serial crystallography for rapid de novo membrane protein structure determination
Assessing and maximizing data quality 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
Making a difference in multi-data-set crystallography : simple and deterministic data-scaling/selection methods
A comparison of some heavy-atom refinement and phasing programs in a test case
Quantifying instrument errors in macromolecular X-ray data sets
Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach
SUPERIMPOSE - a program for the unambiguous structural superposition of spatially related molecules, including macromolecules
Breaking the indexing ambiguity in serial crystallography
Identification of rogue datasets in serial crystallography
Computing in macromolecular crystallography using a parallel architecture
In situ serial crystallography for rapid de novo membrane protein structure determination
Assessing and maximizing data quality 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
Making a difference in multi-data-set crystallography : simple and deterministic data-scaling/selection methods
A comparison of some heavy-atom refinement and phasing programs in a test case
Quantifying instrument errors in macromolecular X-ray data sets
Simulation of X-ray frames from macromolecular crystals using a ray-tracing approach