Preliminary investigation of crystals of the neutral lipase from Pseudomonas fluorescens.
The neutral lipase from the bacteria Pseudomonas fluorescens, marketed under the trade name LpL-200S, has been crystallized in a form suitable for X-ray diffraction analysis from 35% n-propanol at pH 8.5. The crystals are monoclinic prisms and are of space group C2 with a = 91.00 A, b = 47.17 A, c = 35.21 A and beta = 121.43 degrees. There is one molecule of the protein as the asymmetric unit of the crystals. The diffraction pattern extends to at least 1.6 A resolution and the crystals are extremely robust in terms of X-ray exposure.
Department of Biochemistry, University of California, Riverside 92521.
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Larson
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Day
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Greenwood
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Oliver
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Rubingh
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McPherson
D003460:Crystallization; D008049:Lipase / Q000648:ultrastructure*; D011551:Pseudomonas fluorescens / Q000201:enzymology* / Q000648:ultrastructure; D014961:X-Ray Diffraction
D008049:Lipase