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EM data and each annotation group defined an OCP project that can be queried, downloaded, or visualized independently.
CATMAID includes an overlay capability to place layers of annotations on top of EM data and controls to adjust transparency of layers.
In this section, we present scene reconstruction results for the partial sparsity technique using numerical EM data and provide performance comparison with the subspace projection approach for both full and reduced data volumes.
The left columns display the representative SEM micrographs from each volume of EM data, and the right columns display the 3D rendering of boxed areas of the left with the yellow spheres for mitochondria and purple layers for APEX2-induced EM contrast.
A more extensive study of repeatability was carried out by Huang and Cogbill [11] in which they concluded that spatially consistent flight paths are required for repeatability analysis of the EM data, and that this analysis is more meaningful if the apparent resistivity is used instead of the EM response itself.
We like to thank Heidi de Wit for critical discussion of the EM data and Robbert Zalm, Joost Hoetjes and Joke Wortel for invaluable technical assistance.
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L.B. performed RNC purifications, L.B. and S.W. processed the cryo-EM data and built molecular models for the nascent chain and SecYE.
We thank H. Li and W. Lü for help with analysing the cryo-EM data and for advice on refinement, L. Bai and Z. Yuan for advice on 3D reconstruction, V. Falconieri for assistance with figure preparation, the HPC team at VARI for computational support, D. Nadziejka for manuscript editing, and B. Dickson for consultation on molecular dynamics simulation.
S.M. carried out protein purification, collected and processed the cryo-EM data, and built and refined the models, with assistance from A.R.A. R.D. and K.W.M. designed and analysed the electrophysiological experiments, which were performed by R.D. T.U., E.P. and J.S. designed and generated Mb38.
Our method should be useful in the objective analysis of structures of protein assemblies when positions of only Cα positions are available as, for example, in the cases of integration of cryo-EM data and high resolution structures of the components of the assembly.
Cryo-EM data and processing.
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