English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/12505
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:


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
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
Appears in Collections:(IQFR) Artículos
Files in This Item:
There are no files associated with this item.
Show full item record
Review this work

Related articles:

WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.