| Title : Crystallization and preliminary X-ray diffraction studies of a complex of extracellular lipase from Streptomyces rimosus with the inhibitor 3,4-dichloroisocoumarin - Asler_2011_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_67_1378 |
| Author(s) : Asler IL , Pigac J , Vujaklija D , Luic M , Stefanic Z |
| Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 67 :1378 , 2011 |
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Abstract :
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 P2(1), with unit-cell parameters a = 38.1, b = 78.7, c = 56.6 A, beta = 104.5 degrees and probably two molecules in the asymmetric unit. Diffraction data were collected to 1.7 A resolution using synchrotron radiation on the XRD beamline of the Elettra synchrotron, Trieste, Italy. |
| PubMedSearch : Asler_2011_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_67_1378 |
| PubMedID: 22102236 |
Asler IL, Pigac J, Vujaklija D, Luic M, Stefanic Z (2011)
Crystallization and preliminary X-ray diffraction studies of a complex of extracellular lipase from Streptomyces rimosus with the inhibitor 3,4-dichloroisocoumarin
Acta Crystallographica Sect F Struct Biol Cryst Commun
67 :1378
Asler IL, Pigac J, Vujaklija D, Luic M, Stefanic Z (2011)
Acta Crystallographica Sect F Struct Biol Cryst Commun
67 :1378