Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome

D. Borek, M. Jaskolski

Research output: Contribution to journalArticle

15 Scopus citations

Abstract

A new Escherichia coli L-asparaginase belonging to the class of Ntn amidohydrolases has been crystallized using the vapour-diffusion method and PEG 4000 as the precipitant. The crystals belong to the orthorhombic space group P212121 (unit-cell parameters a = 50.3, b = 77.6, c = 148.2 Å) and diffract to 1.65 Å resolution. The structure has been solved by molecular replacement using aspartylglucosaminidase from Flavobacterium meningosepticum as the search model. The asymmetric unit contains four protein chains composed into a dimer of αβ heterodimers, where the subunits α and β are the product of autoproteolytic cleavage of the immature protein.

Original languageEnglish (US)
Pages (from-to)1505-1507
Number of pages3
JournalActa Crystallographica Section D: Biological Crystallography
Volume56
Issue number11
DOIs
StatePublished - Nov 29 2000

ASJC Scopus subject areas

  • Structural Biology

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