TY - JOUR
T1 - Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome
AU - Borek, D.
AU - Jaskolski, M.
PY - 2000
Y1 - 2000
N2 - 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.
AB - 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.
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U2 - 10.1107/S0907444900010076
DO - 10.1107/S0907444900010076
M3 - Article
C2 - 11053866
AN - SCOPUS:0033731155
SN - 0907-4449
VL - 56
SP - 1505
EP - 1507
JO - Acta Crystallographica Section D: Biological Crystallography
JF - Acta Crystallographica Section D: Biological Crystallography
IS - 11
ER -