An organic solvent-tolerant lipase from Bacillus sp. strain 42 was crystallized using the capillary-tube method. The purpose of studying this enzyme was in order to better understand its folding and to characterize its properties in organic solvents. By initially solving its structure in the native state, further studies on protein-solvent interactions could be performed. X-ray data were collected at 2.0 Å resolution using an in-house diffractometer. The estimated crystal dimensions were 0.09 0.19 0.08 mm. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a = 117.41, b = 80.85, c = 99.44 Å, β = 96.40°
Within the BRIDGE T-project on lipases we investigate the structure-function relationships of the li...
The gene encoding thermostable T1 lipase secreted by Geobacillus sp. strain T1 has been overexpresse...
Crystallization of a protein is a process of formation of a solid crystal from a homogeneous solutio...
Purified thermostable recombinant L2 lipase from Bacillus sp. L2 was crystallized by the counter-dif...
The crystallization of proteins makes it possible to determine their structure by X-ray crystallogra...
Single crystals of the lipase from Bacillus subtilis have been obtained using a mixture of polyethyl...
The three-dimensional structure of novel thermostable and organic solvent tolerant ARM lipases was s...
The nature of the enzymes will be denatured in the presence of the organic solvents. Solvents not on...
The discoveries of elastase that actively catalyse a variety of reaction in both aqueous and non-aqe...
The aim of this study was to characterize the organic solvent and detergent tolerant properties of r...
Single crystals of a lipase from Staphylococcus hyicus have been obtained using a combination of 18 ...
An organic solvent-tolerant strain producing lipase was isolated. The optimal pH and temperature wer...
Within the BRIDGE T-project on lipases we investigate the structure-function relationships of the li...
Lipases are ubiquitous in nature and produced by different plants, animals and microorganisms. The...
Bacillus subtilis lipase loses activity above pH 10.5 and below pH 6.0. However, at low pH, i.e. bel...
Within the BRIDGE T-project on lipases we investigate the structure-function relationships of the li...
The gene encoding thermostable T1 lipase secreted by Geobacillus sp. strain T1 has been overexpresse...
Crystallization of a protein is a process of formation of a solid crystal from a homogeneous solutio...
Purified thermostable recombinant L2 lipase from Bacillus sp. L2 was crystallized by the counter-dif...
The crystallization of proteins makes it possible to determine their structure by X-ray crystallogra...
Single crystals of the lipase from Bacillus subtilis have been obtained using a mixture of polyethyl...
The three-dimensional structure of novel thermostable and organic solvent tolerant ARM lipases was s...
The nature of the enzymes will be denatured in the presence of the organic solvents. Solvents not on...
The discoveries of elastase that actively catalyse a variety of reaction in both aqueous and non-aqe...
The aim of this study was to characterize the organic solvent and detergent tolerant properties of r...
Single crystals of a lipase from Staphylococcus hyicus have been obtained using a combination of 18 ...
An organic solvent-tolerant strain producing lipase was isolated. The optimal pH and temperature wer...
Within the BRIDGE T-project on lipases we investigate the structure-function relationships of the li...
Lipases are ubiquitous in nature and produced by different plants, animals and microorganisms. The...
Bacillus subtilis lipase loses activity above pH 10.5 and below pH 6.0. However, at low pH, i.e. bel...
Within the BRIDGE T-project on lipases we investigate the structure-function relationships of the li...
The gene encoding thermostable T1 lipase secreted by Geobacillus sp. strain T1 has been overexpresse...
Crystallization of a protein is a process of formation of a solid crystal from a homogeneous solutio...