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Crystallographic analysis of the Staphylococcus epidermidis lipase involved in esterification in aqueous solution.

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 Rmerge value of 7.3%. The crystals were orthorhombic and belonged to space group P212121, with unit-cell parameters a = 42.07, b = 59.31, c = 171.30?Å, ? = ? = ? = 90°. Solvent-content calculations suggest that there is likely to be one lipase subunit in the asymmetric unit.

SUBMITTER: Liu CH

PROVIDER: S-EPMC5987743 | biostudies-literature | 2018 Jun

REPOSITORIES: biostudies-literature

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Crystallographic analysis of the Staphylococcus epidermidis lipase involved in esterification in aqueous solution.

Liu Cheng Huan CH Chen Yu Ting YT Hou Ming Hon MH Hu Nien Jen NJ Chen Chin Shuh CS Shaw Jei Fu JF

Acta crystallographica. Section F, Structural biology communications 20180521 Pt 6

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<sub>merge</sub> value of 7. ...[more]

PMID: 29870019

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