Crystallization and preliminary crystallographic analysis of N-acetylglucosamine 6-phosphate deacetylase from Escherichia coli

N‐Acetylglucosamine 6‐phosphate deacetylase (E.C. 3.5.1.25), an enzyme from Escherichia coli involved in aminosugar catabolism, has been crystallized by the vapour‐diffusion technique using phosphate as precipitant. X‐ray diffraction experiments show the crystals to belong to the orthorhombic crysta...

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Published inActa crystallographica. Section D, Biological crystallography. Vol. 56; no. 5; pp. 670 - 672
Main Authors Ferreira, F. M., Mendoza-Hernández, G., Calcagno, M. L., Minauro, F., Delboni, L. F., Oliva, G.
Format Journal Article
LanguageEnglish
Published 5 Abbey Square, Chester, Cheshire CH1 2HU, England Munksgaard International Publishers 01.05.2000
Subjects
Amidohydrolases - chemistry
Amidohydrolases - isolation & purification
aminosugar catabolism
Crystallization
Crystallography, X-Ray - methods
Escherichia coli - enzymology
N-acetylglucosamine 6-phosphate deacetylase
Recombinant Proteins - chemistry
Recombinant Proteins - isolation & purification
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Summary:N‐Acetylglucosamine 6‐phosphate deacetylase (E.C. 3.5.1.25), an enzyme from Escherichia coli involved in aminosugar catabolism, has been crystallized by the vapour‐diffusion technique using phosphate as precipitant. X‐ray diffraction experiments show the crystals to belong to the orthorhombic crystal system, with space group P21212. The unit‐cell parameters are a = 82.09 (2), b = 114.50 (1), c = 80.17 (1) Å. The crystals diffract to a maximum resolution of 1.8 Å and an initial data set was collected to 2.0 Å.
Bibliography:ark:/67375/WNG-N4C873W7-R
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ArticleID:AYDGR0984
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:1399-0047
0907-4449
1399-0047
DOI:10.1107/S0907444900003668