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Crystallographic analysis of the Staphylococcus epidermidis lipase involved in esterification in aqueous solution
Author(s) -
Liu Cheng-Huan,
Chen Yu-Ting,
Hou Ming-Hon,
Hu Nien-Jen,
Chen Chin-Shuh,
Shaw Jei-Fu
Publication year - 2018
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 37
ISSN - 2053-230X
DOI - 10.1107/s2053230x18006775
Subject(s) - orthorhombic crystal system , lipase , crystallization , aqueous solution , staphylococcus epidermidis , chemistry , solvent , crystallography , crystal structure , enzyme , organic chemistry , staphylococcus aureus , bacteria , biology , genetics
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.