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1.
Nat Methods ; 21(2): 170-181, 2024 Feb.
Article En | MEDLINE | ID: mdl-37710020

Images document scientific discoveries and are prevalent in modern biomedical research. Microscopy imaging in particular is currently undergoing rapid technological advancements. However, for scientists wishing to publish obtained images and image-analysis results, there are currently no unified guidelines for best practices. Consequently, microscopy images and image data in publications may be unclear or difficult to interpret. Here, we present community-developed checklists for preparing light microscopy images and describing image analyses for publications. These checklists offer authors, readers and publishers key recommendations for image formatting and annotation, color selection, data availability and reporting image-analysis workflows. The goal of our guidelines is to increase the clarity and reproducibility of image figures and thereby to heighten the quality and explanatory power of microscopy data.


Checklist , Publishing , Reproducibility of Results , Image Processing, Computer-Assisted , Microscopy
2.
ArXiv ; 2023 Sep 14.
Article En | MEDLINE | ID: mdl-36824427

Images document scientific discoveries and are prevalent in modern biomedical research. Microscopy imaging in particular is currently undergoing rapid technological advancements. However for scientists wishing to publish the obtained images and image analyses results, there are to date no unified guidelines. Consequently, microscopy images and image data in publications may be unclear or difficult to interpret. Here we present community-developed checklists for preparing light microscopy images and image analysis for publications. These checklists offer authors, readers, and publishers key recommendations for image formatting and annotation, color selection, data availability, and for reporting image analysis workflows. The goal of our guidelines is to increase the clarity and reproducibility of image figures and thereby heighten the quality and explanatory power of microscopy data is in publications.

6.
Nat Methods ; 18(12): 1489-1495, 2021 12.
Article En | MEDLINE | ID: mdl-34862503

For quality, interpretation, reproducibility and sharing value, microscopy images should be accompanied by detailed descriptions of the conditions that were used to produce them. Micro-Meta App is an intuitive, highly interoperable, open-source software tool that was developed in the context of the 4D Nucleome (4DN) consortium and is designed to facilitate the extraction and collection of relevant microscopy metadata as specified by the recent 4DN-BINA-OME tiered-system of Microscopy Metadata specifications. In addition to substantially lowering the burden of quality assurance, the visual nature of Micro-Meta App makes it particularly suited for training purposes.


Metadata , Microscopy, Confocal/instrumentation , Microscopy, Confocal/methods , Microscopy, Fluorescence/instrumentation , Microscopy, Fluorescence/methods , Mobile Applications , Programming Languages , Software , Animals , Cell Line , Computational Biology/methods , Humans , Image Processing, Computer-Assisted , Mice , Pattern Recognition, Automated , Quality Control , Reproducibility of Results , User-Computer Interface , Workflow
8.
Nat Chem Biol ; 10(5): 378-85, 2014 May.
Article En | MEDLINE | ID: mdl-24705592

Hydrogenases catalyze the reversible oxidation of H(2) into protons and electrons and are usually readily inactivated by O(2). However, a subgroup of the [NiFe] hydrogenases, including the membrane-bound [NiFe] hydrogenase from Ralstonia eutropha, has evolved remarkable tolerance toward O(2) that enables their host organisms to utilize H(2) as an energy source at high O(2). This feature is crucially based on a unique six cysteine-coordinated [4Fe-3S] cluster located close to the catalytic center, whose properties were investigated in this study using a multidisciplinary approach. The [4Fe-3S] cluster undergoes redox-dependent reversible transformations, namely iron swapping between a sulfide and a peptide amide N. Moreover, our investigations unraveled the redox-dependent and reversible occurence of an oxygen ligand located at a different iron. This ligand is hydrogen bonded to a conserved histidine that is essential for H(2) oxidation at high O(2). We propose that these transformations, reminiscent of those of the P-cluster of nitrogenase, enable the consecutive transfer of two electrons within a physiological potential range.


Hydrogenase/metabolism , Iron-Sulfur Proteins/metabolism , Oxygen/metabolism , Catalysis , Hydrogen/metabolism , Ligands , Models, Molecular , Oxidation-Reduction
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