Expression, purification and crystallization of Dpr, a ferritin-like protein from the Gram-positive meningitis-associated bacterium Streptococcus suis.
Ferritin-like proteins form a novel family of bacterial proteins with diverse functions, such as DNA binding, iron storage and cell activation. A common structural feature of these proteins is their ability to form spherical dodecamers. Dpr is a ferritin-like protein from the Gram-positive bacterium Streptococcus suis. Full-length and truncated Dpr were expressed and purified as 6xHis-tag fusion proteins. Crystals of truncated Dpr suitable for X-ray diffraction analysis were obtained after the removal of the N-terminal affinity tag by thrombin cleavage. A complete data set to 2.3 A resolution was collected using synchrotron radiation. The crystals belong to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 104.3, b = 137.6, c = 142.1 A and 12 molecules in the asymmetric unit.
D001426:Bacterial Proteins / Q000737:chemistry* / Q000302:isolation & purification; D001483:Base Sequence; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray / Q000379:methods; D017931:DNA Primers; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000302:isolation & purification; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005293:Ferritins / Q000737:chemistry* / Q000302:isolation & purification; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011994:Recombinant Proteins / Q000737:chemistry / Q000302:isolation & purification; D017011:Streptococcus suis / Q000737:chemistry*
D001426:Bacterial Proteins; D017931:DNA Primers; D004268:DNA-Binding Proteins; C414750:Dpr protein, Streptococcus; D011994:Recombinant Proteins; D005293:Ferritins