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Thibault, P. et al. High-resolution scanning X-ray diffraction microscopy.
Thibault, P. et al. High-resolution scanning x-ray diffraction microscopy.
In addition, the structure, morphology, and phase composition of the anodes were studied using X-ray diffraction, microscopy, and Raman spectroscopy.
Here, we investigated the role of lipid composition on penetratin induced membrane perturbations by X-ray diffraction, microscopy and 31P-NMR.
We characterized the local grain deformation behavior using high-resolution electron backscatter diffraction microscopy and an indentation deformation mapping technique.
The method used was far-field high-energy X-ray diffraction microscopy (ff-HEDM), complemented by electron microscopy.
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Next, we used NanoJ-Fluidics for a range of advanced super-resolution imaging protocols, demonstrating its performance and versatility.λLive-cell sub-diffraction microscopy is well established10,11,12.
Sub-diffraction microscopy methods typically map the positions of labeled proteins; however, putting these in the context of membranes and other ultrastructures requires EM.
The C-technology, massive parallel sequencing and sub-diffraction microscopy allow us to obtain unprecedented insight in the three dimensional organization of the genome.
The strength of various sub-diffraction microscopy methods to dissect the nanoscale architecture of multi-protein complexes has been exemplified recently in the case of neuronal synapses (Dani et al., 2010), adhesion complexes (Kanchanawong et al., 2010), centrosomes (Lau et al., 2012; Lawo et al., 2012; Mennella et al., 2012) and the nuclear pore complex (Szymborska et al., 2013).
The microstructure and surface morphology of LZO buffer layers were studied by X-ray diffraction, optical microscopy, field emission scanning electron microscopy and atomic force microscopy.
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