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Protein preparation and preliminary X-ray crystallographic analysis of a putative glucosamine 6-phosphate deaminase from Streptococcus mutants.
- Source :
-
Acta crystallographica. Section F, Structural biology and crystallization communications [Acta Crystallogr Sect F Struct Biol Cryst Commun] 2007 Sep 01; Vol. 63 (Pt 9), pp. 809-11. Date of Electronic Publication: 2007 Aug 31. - Publication Year :
- 2007
-
Abstract
- The SMU.636 protein from Streptococcus mutans is a putative glucosamine 6-phosphate deaminase with 233 residues. The smu.636 gene was PCR-amplified from S. mutans genomic DNA and cloned into the expression vector pET-28a(+). The resultant His-tagged fusion protein was expressed in Escherichia coli and purified to homogeneity in two steps. Crystals of the fusion protein were obtained by the hanging-drop vapour-diffusion method. The crystals diffracted to 2.4 A resolution and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 53.83, b = 82.13, c = 134.70 A.
- Subjects :
- Aldose-Ketose Isomerases genetics
Aldose-Ketose Isomerases isolation & purification
Amino Acid Sequence
Bacterial Proteins chemistry
Bacterial Proteins isolation & purification
Conserved Sequence
Crystallization
Crystallography, X-Ray
Molecular Sequence Data
Polymerase Chain Reaction
Recombinant Proteins chemistry
Recombinant Proteins isolation & purification
Sequence Alignment
Aldose-Ketose Isomerases chemistry
Streptococcus mutans enzymology
Subjects
Details
- Language :
- English
- ISSN :
- 1744-3091
- Volume :
- 63
- Issue :
- Pt 9
- Database :
- MEDLINE
- Journal :
- Acta crystallographica. Section F, Structural biology and crystallization communications
- Publication Type :
- Academic Journal
- Accession number :
- 17768362
- Full Text :
- https://doi.org/10.1107/S1744309107040304