Crystallization of type I chloramphenicol acetyltransferase: An approach based on the concept of ionic strength reducers

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dc.contributor.authorAndreeva A.
dc.contributor.authorBorissova B.
dc.contributor.authorMironova R.
dc.contributor.authorGlykos N.
dc.contributor.authorKotsifaki D.
dc.contributor.authorIvanov I.
dc.contributor.authorKrysteva M.
dc.contributor.authorKokkinidis M.
dc.date.accessioned2024-07-10T14:27:02Z
dc.date.accessioned2024-07-10T14:46:54Z
dc.date.available2024-07-10T14:27:02Z
dc.date.available2024-07-10T14:46:54Z
dc.date.issued2000-01-01
dc.description.abstractChloramphenicol acetyltransferase (CAT) is responsible for bacterial resistance to chloramphenicol. It catalyzes inactivation of the antibiotic by acetyl-group transfer from acetyl CoA to one or both hydroxyl groups of chloramphenicol. Type I CAT possesses some unique properties which are not observed in other CAT variants. Type I CAT overexpressed in Escherichia coli was purified and crystals with a resolution limit of 2.22 Å have been obtained using a novel procedure which is based on the concept of 'ionic strength reducers'. The crystals have the symmetry of space group P1 and unit-cell parameters a = 96.46, b = 113.86, c= 114.21 Å, α= 119.9, β= 94.1, γ = 98.6°. These dimensions are consistent with four to six trimers per unit cell, corresponding to a solvent fraction ranging from 65 to 47%.
dc.identifier.doi10.1107/S090744499901481X
dc.identifier.issn0907-4449
dc.identifier.scopusSCOPUS_ID:0033972685en
dc.identifier.urihttps://rlib.uctm.edu/handle/123456789/71
dc.language.isoen
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=0033972685&origin=inward
dc.titleCrystallization of type I chloramphenicol acetyltransferase: An approach based on the concept of ionic strength reducers
dc.typeArticle
oaire.citation.issue1
oaire.citation.volume56
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