Forthcoming article in Acta Crystallographica Section D Structural Biology
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Acta Crystallographica Section D: Structural Biology welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules and the methods used to determine them. Reports on new protein structures are particularly encouraged, as are structure-function articles that could include crystallographic binding studies, or structural analysis of mutants or other modified forms of a known protein structure. The key criterion is that such articles should present new insights into biology, chemistry or structure. Articles on crystallographic methods should be oriented towards biological crystallography, and may include new approaches to any aspect of structure determination or analysis. Articles on the crystallization of biological molecules will be accepted providing that these focus on new methods or other features that are of general importance or applicability.en-gbCopyright (c) 2024 International Union of CrystallographyInternational Union of CrystallographyInternational Union of Crystallographyurn:issn:0907-4449text/htmlActa Crystallographica Section D Structural Biologytexthttps://journals.iucr.orgActa Crystallographica Section D: Structural Biology welcomes the submission of articles covering any aspect of structural biology, with a particular emphasis on the structures of biological macromolecules and the methods used to determine them. Reports on new protein structures are particularly encouraged, as are structure-function articles that could include crystallographic binding studies, or structural analysis of mutants or other modified forms of a known protein structure. The key criterion is that such articles should present new insights into biology, chemistry or structure. Articles on crystallographic methods should be oriented towards biological crystallography, and may include new approaches to any aspect of structure determination or analysis. Articles on the crystallization of biological molecules will be accepted providing that these focus on new methods or other features that are of general importance or applicability.1daily2002-01-01T00:00+00:00Copyright (c) 2024 International Union of CrystallographyActa Crystallographica Section D Structural Biologymed@iucr.orgurn:issn:0907-4449Forthcoming article in Acta Crystallographica Section D Structural Biologyhttp://journals.iucr.org/logos/rss10d.gif
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Still imageScaling and merging macromolecular diffuse scattering with mdx2
http://journals.iucr.org/d/services/forthcoming.html#qq5001
Mdx2 is a Python toolkit for processing diffuse scattering data from macromolecular crystals. Here, the multi-crystal scaling and merging procedures implemented in the latest version of mdx2 are described. A high-redundancy data set from cubic insulin is processed to reveal weak scattering features.doi:10.1107/S2059798324002705enCopyright (c) 2024 International Union of Crystallographytext/htmlScaling and merging macromolecular diffuse scattering with mdx2textDIFFUSE SCATTERING; MACROMOLECULAR CRYSTALLOGRAPHY; DATA PROCESSING; SOFTWARE; RECIPROCAL-SPACE MAPPINGMeisburger and AndoInternational Union of Crystallographyurn:issn:2059-7983Mdx2 is a Python toolkit for processing diffuse scattering data from macromolecular crystals. Here, the multi-crystal scaling and merging procedures implemented in the latest version of mdx2 are described. A high-redundancy data set from cubic insulin is processed to reveal weak scattering features.Mdx2 is a Python toolkit for processing diffuse scattering data from macromolecular crystals. Here, the multi-crystal scaling and merging procedures implemented in the latest version of mdx2 are described. A high-redundancy data set from cubic insulin is processed to reveal weak scattering features.Mononuclear binding and catalytic activity of europium(III) and gadolinium(III) at the active site of the model metalloenzyme phosphotriesterase
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The crystal structures of europium(III)- and gadolinium(III)-bound phosphotriesterase are presented along with esterase activity data for the lanthanide-bound enzymes.doi:10.1107/S2059798324002316enCopyright (c) 2024 International Union of Crystallographytext/htmlMononuclear binding and catalytic activity of europium(III) and gadolinium(III) at the active site of the model metalloenzyme phosphotriesterasetextLANTHANIDES; PHOSPHOTRIESTERASE; ANOMALOUS SCATTERINGCallum W. Breeze et al.International Union of Crystallographyurn:issn:2059-7983The crystal structures of europium(III)- and gadolinium(III)-bound phosphotriesterase are presented along with esterase activity data for the lanthanide-bound enzymes.The crystal structures of europium(III)- and gadolinium(III)-bound phosphotriesterase are presented along with esterase activity data for the lanthanide-bound enzymes.Efficient in situ screening of and data collection from microcrystals in crystallization plates
http://journals.iucr.org/d/services/forthcoming.html#wa5148
A sample- and time-efficient method to obtain serial crystallography data from batch-grown microcrystals dispensed as drops on a 96-well crystallization plate is described. This offers a versatile method to obtain low-dose room-temperature structures and guide the optimization of microcrystallization for synchrotron and XFEL serial crystallography experiments.doi:10.1107/S2059798324001955enCopyright (c) 2024 International Union of Crystallographytext/htmlEfficient in situ screening of and data collection from microcrystals in crystallization platestextSERIAL CRYSTALLOGRAPHY; IN SITU DATA COLLECTION; PEROXIDASE; RADIATION DAMAGE; MICROCRYSTALSAmy J. Thompson et al.International Union of Crystallographyurn:issn:2059-7983A sample- and time-efficient method to obtain serial crystallography data from batch-grown microcrystals dispensed as drops on a 96-well crystallization plate is described. This offers a versatile method to obtain low-dose room-temperature structures and guide the optimization of microcrystallization for synchrotron and XFEL serial crystallography experiments.A sample- and time-efficient method to obtain serial crystallography data from batch-grown microcrystals dispensed as drops on a 96-well crystallization plate is described. This offers a versatile method to obtain low-dose room-temperature structures and guide the optimization of microcrystallization for synchrotron and XFEL serial crystallography experiments.Tomo Live: an on-the-fly reconstruction pipeline to judge data quality for cryo-electron tomography workflows
http://journals.iucr.org/d/services/forthcoming.html#qv5004
To simplify the cryo-electron tomography workflow and make this technique more accessible to all researchers, the Tomo Live software has been developed, which performs on-the-fly reconstruction of tilt series, enabling real-time data-quality monitoring, curation and export.doi:10.1107/S2059798324001840enCopyright (c) 2024 International Union of Crystallographytext/htmlTomo Live: an on-the-fly reconstruction pipeline to judge data quality for cryo-electron tomography workflowstextELECTRON TOMOGRAPHY; REAL-TIME PROCESSING; CRYO-ET; TOMO LIVEMaxime Comet et al.International Union of Crystallographyurn:issn:2059-7983To simplify the cryo-electron tomography workflow and make this technique more accessible to all researchers, the Tomo Live software has been developed, which performs on-the-fly reconstruction of tilt series, enabling real-time data-quality monitoring, curation and export.To simplify the cryo-electron tomography workflow and make this technique more accessible to all researchers, the Tomo Live software has been developed, which performs on-the-fly reconstruction of tilt series, enabling real-time data-quality monitoring, curation and export.VitroJet: new features and case studies
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This paper presents recent technical improvements to the VitroJet and the benefits that it brings to the cryo-EM workflow, as well as a wide variety of case studies. This illustrates the advancement of the VitroJet into an instrument that enables accurate control and reproducibility, demonstrating its suitability for time-efficient cryo-EM structure determination.doi:10.1107/S2059798324001852enCopyright (c) 2024 International Union of Crystallographytext/htmlVitroJet: new features and case studiestextCRYO-EM; VITROJET; ICE THICKNESS; PIN PRINTING; JET VITRIFICATIONRene J. M. Henderikx et al.International Union of Crystallographyurn:issn:2059-7983This paper presents recent technical improvements to the VitroJet and the benefits that it brings to the cryo-EM workflow, as well as a wide variety of case studies. This illustrates the advancement of the VitroJet into an instrument that enables accurate control and reproducibility, demonstrating its suitability for time-efficient cryo-EM structure determination.This paper presents recent technical improvements to the VitroJet and the benefits that it brings to the cryo-EM workflow, as well as a wide variety of case studies. This illustrates the advancement of the VitroJet into an instrument that enables accurate control and reproducibility, demonstrating its suitability for time-efficient cryo-EM structure determination.Structural determination and modeling of ciliary microtubules
http://journals.iucr.org/d/services/forthcoming.html#ih5006
This review describes how electron-microscopy methods have helped to reveal the structure of the ciliary axoneme.doi:10.1107/S2059798324001815enCopyright (c) 2024 International Union of Crystallographytext/htmlStructural determination and modeling of ciliary microtubulestextCRYO-EM; CRYO-ET; CILIA; AXONEMES; MICROTUBULESWalton, Doran and BrownInternational Union of Crystallographyurn:issn:2059-7983This review describes how electron-microscopy methods have helped to reveal the structure of the ciliary axoneme.This review describes how electron-microscopy methods have helped to reveal the structure of the ciliary axoneme.EMinsight: a tool to capture cryoEM microscope configuration and experimental outcomes for analysis and deposition
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EMinsight is a Python-based tool for systematically mining metadata from single-particle analysis cryoEM experiments. The capture and analysis of metadata facilitates the assessment of instrument performance, provides concise reporting of experiment performance and sample quality by analysing preprocessing results, and gathers metadata for deposition. It is envisaged that this approach will benefit the microscope operator, facility managers, database developers and users.doi:10.1107/S2059798324001578enCopyright (c) 2024 International Union of Crystallographytext/htmlEMinsight: a tool to capture cryoEM microscope configuration and experimental outcomes for analysis and depositiontextEMINSIGHT; CRYOEM; DATA MINING; DEPOSITION; MACHINE LEARNINGDaniel Hatton et al.International Union of Crystallographyurn:issn:2059-7983EMinsight is a Python-based tool for systematically mining metadata from single-particle analysis cryoEM experiments. The capture and analysis of metadata facilitates the assessment of instrument performance, provides concise reporting of experiment performance and sample quality by analysing preprocessing results, and gathers metadata for deposition. It is envisaged that this approach will benefit the microscope operator, facility managers, database developers and users.EMinsight is a Python-based tool for systematically mining metadata from single-particle analysis cryoEM experiments. The capture and analysis of metadata facilitates the assessment of instrument performance, provides concise reporting of experiment performance and sample quality by analysing preprocessing results, and gathers metadata for deposition. It is envisaged that this approach will benefit the microscope operator, facility managers, database developers and users.AlphaFold-assisted structure determination of a bacterial protein of unknown function using X-ray and electron crystallography
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The structure determination of a small protein of unknown function by molecular replacement using a search model predicted by new machine-learning methods is reported. Notably, the approach was successful using electron diffraction data collected from a protein microcrystal, highlighting a potentially important new route for structure determination.doi:10.1107/S205979832400072XenCopyright (c) 2024 International Union of Crystallographytext/htmlAlphaFold-assisted structure determination of a bacterial protein of unknown function using X-ray and electron crystallographytextELECTRON DIFFRACTION; PROTEIN STRUCTURE PREDICTION; ALPHAFOLD; BACTERIAL PROTEINS; MOLECULAR REPLACEMENTJustin E. Miller et al.International Union of Crystallographyurn:issn:2059-7983The structure determination of a small protein of unknown function by molecular replacement using a search model predicted by new machine-learning methods is reported. Notably, the approach was successful using electron diffraction data collected from a protein microcrystal, highlighting a potentially important new route for structure determination.The structure determination of a small protein of unknown function by molecular replacement using a search model predicted by new machine-learning methods is reported. Notably, the approach was successful using electron diffraction data collected from a protein microcrystal, highlighting a potentially important new route for structure determination.