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Title

Crystallization and preliminary X-ray diffraction studies of the BTL2 lipase from extremophilic microorganism Bacillus thermocatenulatus

AuthorsCarrasco-López, César ; Godoy, César; Rivas, Blanca de las ; Fernández-Lorente, Gloria ; Palomo, José Miguel ; Guisán Seijas, José Manuel; Fernández-Lafuente, Roberto ; Martínez-Ripoll, Martín ; Hermoso, Juan A.
KeywordsBacillus thermocatenulatus
Lipases
Issue Date2008
PublisherInternational Union of Crystallography
CitationActa Crystallographica (2008) F64, 1043-1045
AbstractBacillus thermocatenulatus lipase 2 (BTL2) is a thermoalkalophilic lipase that has been reported as an enantioselective biocatalyst for diverse reactions and that heads a group of enzymes that share high resistance towards many inactivation agents (heat, organic solvents, pH etc.). This makes BTL2 an important research target because of its potential industrial applications. BTL2 was cloned and overexpressed in Escherichia coli, purified and concentrated for crystallization using the sitting-drop vapour-diffusion method at 291 K. Crystals grew from a mixture of 13% MPD and 0.2 M ammonium acetate in 0.05 M sodium citrate pH 5.5-5.6. The crystals, which belonged to the orthorhombic space group I222 with unit-cell parameters a = 73.07, b = 129.08, c = 127.49 Å, allowed the collection of an X-ray data set to 2.2 Å resolution.
Publisher version (URL)http://dx.doi.org/10.1107/S1744309108031928
URIhttp://hdl.handle.net/10261/12505
DOI10.1107/S1744309108031928
ISSN1744-3091
Appears in Collections:(IQFR) Artículos
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