Expression, purification and crystallization of Dpr, a ferritin-like protein from the Gram-positive meningitis-associated bacterium Streptococcus suis

: Haataja S, Penttinen A, Pulliainen AT, Tikkanen K, Finne J, Papageorgiou AC

: 2002

: Acta Crystallographica Section D: Biological Crystallography

: Acta crystallographica. Section D, Biological crystallography

: Acta Crystallogr D Biol Crystallogr

: 58

: Pt 10 Pt 2

: 1851

: 3

: 0907-4449

DOI: https://doi.org/10.1107/S0907444902012970

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.