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 CrystallographyActa Crystallographica Section D Structural Biologyhttps://journals.iucr.orgtext/htmltextActa 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.urn:issn:0907-44492002-01-01T00:00+00:001dailyCopyright (c) 2024 International Union of Crystallographyurn:issn:0907-4449med@iucr.orgActa Crystallographica Section D Structural BiologyForthcoming article in Acta Crystallographica Section D Structural Biologyhttp://journals.iucr.org/logos/rss10d.gif
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Still imageMononuclear binding and catalytic activity of europium(III) and gadolinium(III) at the active site of the model metalloenzyme phosphotriesterase
http://journals.iucr.org/d/services/forthcoming.html#jb5062
The crystal structures of europium(III)- and gadolinium(III)-bound phosphotriesterase are presented along with esterase activity data for the lanthanide-bound enzymes.Callum W. Breeze et al.Copyright (c) 2024 International Union of CrystallographyenThe crystal structures of europium(III)- and gadolinium(III)-bound phosphotriesterase are presented along with esterase activity data for the lanthanide-bound enzymes.Mononuclear binding and catalytic activity of europium(III) and gadolinium(III) at the active site of the model metalloenzyme phosphotriesteraseurn:issn:2059-7983text/htmltextThe crystal structures of europium(III)- and gadolinium(III)-bound phosphotriesterase are presented along with esterase activity data for the lanthanide-bound enzymes.International Union of Crystallographydoi:10.1107/S2059798324002316LANTHANIDES; PHOSPHOTRIESTERASE; ANOMALOUS SCATTERINGEfficient in situ screening of and data collection from microcrystals in crystallization plates
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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.Amy J. Thompson et al.Copyright (c) 2024 International Union of CrystallographyenA 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.Efficient in situ screening of and data collection from microcrystals in crystallization platesurn:issn:2059-7983text/htmltextA 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.International Union of Crystallographydoi:10.1107/S2059798324001955SERIAL CRYSTALLOGRAPHY; IN SITU DATA COLLECTION; PEROXIDASE; RADIATION DAMAGE; MICROCRYSTALSTomo 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.Maxime Comet et al.Copyright (c) 2024 International Union of CrystallographyenTo 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.Tomo Live: an on-the-fly reconstruction pipeline to judge data quality for cryo-electron tomography workflowsurn:issn:2059-7983text/htmltextTo 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.International Union of Crystallographydoi:10.1107/S2059798324001840ELECTRON TOMOGRAPHY; REAL-TIME PROCESSING; CRYO-ET; TOMO LIVEVitroJet: new features and case studies
http://journals.iucr.org/d/services/forthcoming.html#ih5005
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.Rene J. M. Henderikx et al.Copyright (c) 2024 International Union of CrystallographyenThis 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.VitroJet: new features and case studiesurn:issn:2059-7983text/htmltextThis 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.International Union of Crystallographydoi:10.1107/S2059798324001852CRYO-EM; VITROJET; ICE THICKNESS; PIN PRINTING; JET VITRIFICATIONStructural determination and modeling of ciliary microtubules
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This review describes how electron-microscopy methods have helped to reveal the structure of the ciliary axoneme.Walton, Doran and BrownCopyright (c) 2024 International Union of CrystallographyenThis review describes how electron-microscopy methods have helped to reveal the structure of the ciliary axoneme.Structural determination and modeling of ciliary microtubulesurn:issn:2059-7983text/htmltextThis review describes how electron-microscopy methods have helped to reveal the structure of the ciliary axoneme.International Union of Crystallographydoi:10.1107/S2059798324001815CRYO-EM; CRYO-ET; CILIA; AXONEMES; MICROTUBULESEMinsight: 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.Daniel Hatton et al.Copyright (c) 2024 International Union of CrystallographyenEMinsight 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: a tool to capture cryoEM microscope configuration and experimental outcomes for analysis and depositionurn:issn:2059-7983text/htmltextEMinsight 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.International Union of Crystallographydoi:10.1107/S2059798324001578CRYOEM; DATA MINING; DEPOSITION; MACHINE LEARNINGAlphaFold-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.Justin E. Miller et al.Copyright (c) 2024 International Union of CrystallographyenThe 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.AlphaFold-assisted structure determination of a bacterial protein of unknown function using X-ray and electron crystallographyurn:issn:2059-7983text/htmltextThe 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.International Union of Crystallographydoi:10.1107/S205979832400072XELECTRON DIFFRACTION; PROTEIN STRUCTURE PREDICTION; ALPHAFOLD; BACTERIAL PROTEINS; MOLECULAR REPLACEMENT