Unknown

Dataset Information

0

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

ABSTRACT: Bacillus 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 A, allowed the collection of an X-ray data set to 2.2 A resolution.

SUBMITTER: Carrasco-Lopez C 

PROVIDER: S-EPMC2581703 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

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

Carrasco-López César C   Godoy Cesar C   de las Rivas Blanca B   Fernández-Lorente Gloria G   Palomo José M JM   Guisán José M JM   Fernández-Lafuente Roberto R   Martínez-Ripoll Martín M   Hermoso Juan A JA  

Acta crystallographica. Section F, Structural biology and crystallization communications 20081031 Pt 11

Bacillus 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-dro  ...[more]

Similar Datasets

Unknown Crystallization and preliminary X-ray diffraction studies on the bicupin YwfC from Bacillus subtilis.
| S-EPMC2225362 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction studies of Staphylococcus aureus homoserine dehydrogenase.
| S-EPMC3818036 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction studies of La1 from Liocheles australasiae.
| S-EPMC4089531 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction studies of a complex of extracellular lipase from Streptomyces rimosus with the inhibitor 3,4-dichloroisocoumarin.
| S-EPMC3212455 | biostudies-literature
Unknown Purification, crystallization and preliminary X-ray diffraction experiment of nattokinase from Bacillus subtilis natto.
| S-EPMC2998380 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction studies of sortase A from Streptococcus pneumoniae.
| S-EPMC3212360 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction studies of ferredoxin reductase from Leptospira interrogans.
| S-EPMC2242957 | biostudies-literature
Unknown Purification, crystallization and preliminary X-ray diffraction studies of parakeet (Psittacula krameri) haemoglobin.
| S-EPMC2765893 | biostudies-literature
Unknown Crystallization and preliminary X-ray diffraction analysis of the arginine repressor ArgR from Bacillus halodurans.
| S-EPMC4356304 | biostudies-literature
Unknown Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of YvoA from Bacillus subtilis.
| S-EPMC2664774 | biostudies-literature