Crystallization and preliminary X-ray diffraction studies of a complex of extracellular lipase from Streptomyces rimosus with the inhibitor 3,4-dichloroisocoumarin

• Published in: Acta crystallographica. Section F, Structural biology and crystallization communications Vol. 67; no. 11; pp. 1378 - 1381
• Main Authors: Leščić Ašler, Ivana, Pigac, Jasenka, Vujaklija, Dušica, Luić, Marija, Štefanić, Zoran
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01.11.2011
• Subjects: 3,4‐dichloroisocoumarin; 4-dichloroisocoumarin; Asymmetry; Coumarins - chemistry; Crystallization; Crystallization Communications; Crystallography, X-Ray; Diffraction; Enzyme Inhibitors - chemistry; Extracellular Space - enzymology; Inhibitors; Lipase; Lipase - chemistry; lipases; Recombinant; SGNH hydrolases; Streptomyces - enzymology; Streptomyces rimosus; Synchrotrons
• ISSN: 1744-3091; 1744-3091
• DOI: 10.1107/S1744309111032222

A recombinant lipase (triacylglycerol acylhydrolase; EC 3.1.1.3) from the bacterium Streptomyces rimosus was inhibited by the serine protease inhibitor 3,4‐dichloroisocoumarin and crystallized by the hanging‐drop vapour‐diffusion method at 291 K. The crystals belonged to the monoclinic space group P21, with unit‐cell parameters a = 38.1, b = 78.7, c = 56.6 Å, β = 104.5° and probably two molecules in the asymmetric unit. Diffraction data were collected to 1.7 Å resolution using synchrotron radiation on the XRD beamline of the Elettra synchrotron, Trieste, Italy.