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Catalase is one of the earliest samples studied by EM, but despite extensive efforts spanning decades, the 3D structure of catalase has not been solved using electron diffraction.
Structure determination has been most successful using X-ray diffraction, although 105 of the reported structures were solved using nuclear magnetic resonance (NMR) spectroscopy and a further 14 structures have been solved using electron diffraction, demonstrating the utility of multiple techniques in the membrane protein structure determination tool box [60,61].
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In the second paper, for which David Booth is the first author, the structure of a Rev-RRE-Crm1 complex was solved using cryo-electron microscopy, revealing the existence of a Crm1 dimer interface that is unique among reported Crm1-cargo structures (Booth et al., 2014).
The structure of a human serotonin receptor was solved using a free-electron laser to analyze microcrystals.
Most likely, this will not be solved using cellular cryo-electron microscopy as stand-alone technique, but rather in conjunction with various other technologies such as structural biology, biochemistry, light microscopy, and mass spectrometry-based proteomics.
In the ionospheric model, plasma fluid equations for several major ion species and electrons are solved using the finite difference scheme.
Protein structures are solved using X-ray crystallography, NMR spectroscopy, electron microscopy and (recently) by application of computational approaches, such as homology modeling.
The problem can be solved using short-lived optically excited triplet states delivering the electron spin.
Both models were solved using ode15s.
The problem then was solved using VNS.
The LAP1-VHH-BS1 structure was solved using molecular replacement.
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