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Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome (2000)

Borek, Dominika ; Jaskólski, Mariusz

Copenhagen : International Union of Crystallography (IUCr)

Acta crystallographica 56 (2000), S. 1505-1507

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ISSN: 1399-0047

Source: Crystallography Journals Online : IUCR Backfile Archive 1948-2001

Topics: Chemistry and Pharmacology , Geosciences , Physics

Notes: 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.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1107/S0907444900010076

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