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Structural analysis of the CMG complex by transmission electron microscopy has determined the mechanism of Cdc45 and GINS activation; together these proteins bind across the Mcm2/5 gate and close the discontinuity [ 30].
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Recently, high-resolution transmission electron microscopy (TEM) has determined the atomic arrangement within ferroelectric domains27 and revealed unconventional DWstructures288.
Using electron microscopy, we have determined the structure of the CMG in the presence of ATPγS and a DNA duplex bearing a 3′ single-stranded tail.
Several electron microscopy studies have determined the collagen fibril diameter to be around 100 nm [20,42,43], however, values as low as 20 60 nm have also been reported in the literature [32,44].
Using cryo-electron microscopy, Fernandez-Leiro et al. have determined the ~8 Å resolution structures, in a DNA-bound and DNA-free state, of the holoenzyme catalytic core comprising the E. coli DNA polymerase III α subunit, the DNA sliding clamp β, the exonuclease ε, and the C-terminal domain of the clamp loader subunit τ (τ500).
We have determined the structure of plasma fibronectin by electron microscopy of shadowed specimens.
We have determined the distribution of NHE1 by means of immunofluorescence microscopy and cell-surface biotinylation.
We have determined the structure of the TOM core complex by cryoelectron microscopy (cryo-EM).
We have determined the three-dimensional (3D) structure of the fully assembled human mTORC1 by cryo-electron microscopy (cryo-EM).
Optical microscopy has been used to determine the Arrhenius parameters of the linear growth rate for nano- and microfilaments of about ∼100 nm and larger in diameter.
Magnetic force microscopy has been used to determine the origin and spatial distribution of changes in magnetic properties of an HPM alloy carburised by exposure in an ethylene production furnace.
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