Literature DB >> 9761915

Crystallization and preliminary X-ray analysis of a member of a new family of pectate lyases, PeIL from Erwinia chrysanthemi.

V Shevchik1, M Scott, O Mayans, J Jenkins.   

Abstract

PeIL, a pectate lyase (E.C. 4.2.2.9) from E. chrysanthemi 3937 that is not homologous to the lyases with known structures, has been purified and crystallized by the hanging-drop method using a variety of organic solvents as precipitant. Elongated lathes grown from poly(ethylene glycol) plus isopropanol belong to the space group P212121 with cell dimensions a = 55.5, b = 58.2, c = 16.4 A with a single molecule in the asymmetric unit. Although complete data sets have been collected to 2.3 A resolution, these crystals diffract to at least 1.9 A resolution and are suitable for structure determination. Chunky plates grown using other organic solvents as the precipitant diffracted to 3 A resolution and were partially characterized as a second orthorhombic crystal form with space group P21212 and cell dimensions a = 119.1, b = 140.5 and c = 105.4 A, suggesting four molecules in the asymmetric unit.

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Year:  1998        PMID: 9761915     DOI: 10.1107/s0907444997012043

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Modes of action of five different endopectate lyases from Erwinia chrysanthemi 3937.

Authors:  C Roy; H Kester; J Visser; V Shevchik; N Hugouvieux-Cotte-Pattat; J Robert-Baudouy; J Benen
Journal:  J Bacteriol       Date:  1999-06       Impact factor: 3.490

  1 in total

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