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Purified hUPP1 at 4 mgs/mL was supplemented with 1 mM 5-FU (Sigma) and subject to crystallization screening in conditions similar to those previously identified to successfully crystallize hUPP1 with BAU [20].
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69 proteins that had previously resisted structure determination were subjected to crystallization with in situ proteolysis and ten crystallized in a form that led to structure determination (14.5% success rate).
These residues were subjected to crystallization and re-crystallization in appropriate organic solvents to yield pure crystals of different boswellic acids (BAs).
The growth rates calculated from optical microscopy have been subjected to crystallization regime analysis.
Synthetic solutions were subjected to crystallization, aimed at contributing to the development of a complete biotechnological process, including preliminary xylose-to-xylitol bioconversion in hemicellulose hydrolyzate and final xylitol recovery by crystallization.
Complexes of both Fab proteins with BMPR-IAEC were prepared and subjected to crystallization trials.
After size exclusion, the S1-cleaved Notch1 NRR was concentrated to 10 mg/ml and subjected to crystallization trials.
The target/protease mixtures were allowed to incubate on ice for thirty minutes, at which point they were subjected to crystallization trials.
PPIL1 protein was subjected to crystallization trials in the presence of synthetic peptides encompassing SKIP residues 55 74 and 44 74 (synthesized by Peptide Specialty Laboratories, Heidelberg, Germany).
Purified NX1α III) was concentrated to 10 mg/ml and subjected to crystallization screening via the hanging-drop vapor diffusion method using a Wizard I & II screening kit (Emerald BioSystems).
The CIDRα1 EPCR complexes were next subjected to crystallization trials.
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