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- W2804080214 abstract "The Staphylococcus epidermidis lipase (SeLip, GehC) can be used in flavour-compound production via esterification in aqueous solution. This study reports the crystallization and crystallographic analysis of recombinant GehC (rGehC; Lys303–Lys688) with a molecular weight of 43 kDa. rGehC was crystallized at 293 K using PEG 10 000 as a precipitant, and a 99.9% complete native data set was collected from a cooled crystal at 77 K to a resolution of 1.9 Å with an overall R merge value of 7.3%. The crystals were orthorhombic and belonged to space group P 2 1 2 1 2 1 , with unit-cell parameters a = 42.07, b = 59.31, c = 171.30 Å, α = β = γ = 90°. Solvent-content calculations suggest that there is likely to be one lipase subunit in the asymmetric unit." @default.
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- W2804080214 date "2018-05-21" @default.
- W2804080214 modified "2023-10-15" @default.
- W2804080214 title "Crystallographic analysis of the <i>Staphylococcus epidermidis</i> lipase involved in esterification in aqueous solution" @default.
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- W2804080214 doi "https://doi.org/10.1107/s2053230x18006775" @default.
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