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The development and use of more sensitive analytical instrumentation, especially inductively coupled plasma mass spectrometry (ICP-MS), has resulted in determinations of Pb in plasma and serum specimens with much lower detection limits and with better accuracy.
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Their experiments resulted in determination of the smallest instantaneous displacement discriminable from a continuous drift and shortest motion stop discriminable from a continuous drift.
They performed experiments which resulted in determination of (i) smallest instantaneous displacement (infinite velocity) discriminable from a continuous drift, (ii) shortest motion stop discriminable from a continuous drift. .
GC and GC MS analysis of the essential oil were resulted in determination 22 different compounds, representing 99.61% of total oil.
Tomographic inversion of the first arrival grid data resulted in determination of an accurate three-dimensional (3-D) velocity field, to a depth of 4 km.
Fast Fourier transformation data processing of resonance frequency data resulted in determination of a maximum resonance frequency values allowing calculation of implant stability quotient (ISQ) values using the Osstell algorithm.
The direct titration curves were well approximated by the McGhee-von Hippel model that resulted in determination of the binding constant (∼1 × 106 M−1), apparent ligand size (∼10), cooperativity parameter (∼11) as well as the enthalpies of binding and ligand-ligand interaction.
Interlaboratory comparative studies resulted in determination of a reference value for the ethene formed after thermal decomposition of the surface compound ((2.12 ± 0.14) ng per fibre).
Subsequent proceeding of Cufflinks output with Cuffcompare, Cuffmerge and Cuffdiff with default settings resulted in determination of differentially expressed transcripts after data normalization in order to correct for differences in both library sizes and gene length.
The development of direct detectors and more stable microscopes, combined with new data processing algorithms and improved specimen preparations, has recently resulted in determination at atomic resolution of several protein structures, including a eukaryotic ion channel, by electron microscopy (EM), using approaches not reliant on symmetry or 2D crystallisation [21,22,23].
In order to reduce the resulting bias, forest plots were calculated and the weight was adjusted on the raw data, resulting in determination of the random effect.
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