Literature DB >> 1942065

Preliminary investigation of crystals of the neutral lipase from Pseudomonas fluorescens.

S Larson1, J Day, A Greenwood, J Oliver, D Rubingh, A McPherson.   

Abstract

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.

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Year:  1991        PMID: 1942065     DOI: 10.1016/0022-2836(91)90732-l

Source DB:  PubMed          Journal:  J Mol Biol        ISSN: 0022-2836            Impact factor:   5.469


  1 in total

1.  Immobilization of Amano lipase AK from Pseudomonas fluorescens on different types of chitosan-containing supports: use in the kinetic resolution of rac-indanol.

Authors:  Thiago de Sousa Fonseca; Ulisses Marcondes Freire de Oliveira; Maria da Conceição Ferreira de Oliveira; Telma Leda Gomes de Lemos; Marcos Reinaldo da Silva; Nathalia Saraiva Rios; Luciana Rocha Barros Gonçalves; Marcos Carlos de Mattos
Journal:  Bioprocess Biosyst Eng       Date:  2021-01-03       Impact factor: 3.210

  1 in total

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