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 A resolution using an in-house diffractometer. The estimated crystal dimensions were 0.09x0.19x0.08 mm. The crystal belonged to the monoclinic space group C2, with unit-cell parameters a=117.41, b=80.85, c=99.44 A, beta=96.40 degrees .
        
Representative scheme of Bacterial_lip_FamI.5 structure and an image from PDBsum server
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4FKB Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
4FKBFold classification based on Structure-Structure alignment of Proteins - FSSP server