Expression, purification and X-ray characterization of residues 18-230 from the pneumococcal histidine triad protein A (PhtA) from Streptococcus pneumoniae.
A fragment of the Streptococcus pneumoniae PhtA gene product (residues 18-230) was cloned and overexpressed in Escherichia coli. The purified protein was crystallized using the sitting-drop vapour-diffusion technique. Crystals belong to the monoclinic space group C2, with unit-cell parameters a = 62.19, b = 35.9, c = 72.54 A, beta = 90.01 degrees. The crystals diffract X-rays to beyond 1.2 A resolution.
Riboldi-Tunnicliffe
Alan
A
Division of Infection and Immunity (IBLS), University of Glasgow, Joseph Black Building, University Avenue, Glasgow G12 8QQ, Scotland. atunni@chem.gla.ac.uk
Bent
Colin J
CJ
Isaacs
Neil W
NW
Mitchell
Timothy J
TJ
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics; D006867:Hydrolases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification*; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification; D011487:Protein Conformation; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D013296:Streptococcus pneumoniae / Q000737:chemistry*
D010446:Peptide Fragments; D011994:Recombinant Proteins; C097552:histidine triad protein; D006867:Hydrolases