Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of HP1352, a putative DNA methyltransferase in Helicobacter pylori.
The putative methyltransferase gene HP1352 from Helicobacter pylori strain 26695 was heterologously expressed in Escherichia coli. The 359-amino-acid gene product was purified and crystallized. The crystals belong to space group I2(1)2(1)2(1) and show diffraction to at least 2.5 A resolution. The unit-cell parameters are a = 69.6, b = 86.6, c = 140.0 A. A greater than 90% complete native data set has been collected and structure determination using the molecular-replacement method is ongoing.
Schirwitz
Katja
K
EMBL Hamburg Outstation, Germany.
Lundin
Annelie
A
Skoglund
Anna
A
Krabbe
Margareta
M
Engstrand
Lars
L
Enroth
Cristofer
C
D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D015254:DNA Modification Methylases / Q000737:chemistry*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D005798:Genes, Bacterial; D016480:Helicobacter pylori / Q000201:enzymology*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D015254:DNA Modification Methylases; C478741:HP1352 protein, Helicobacter pylori