A1 Refereed original research article in a scientific journal
Expression, purification and crystallization of Dpr, a ferritin-like protein from the Gram-positive meningitis-associated bacterium Streptococcus suis
Authors: Haataja S, Penttinen A, Pulliainen AT, Tikkanen K, Finne J, Papageorgiou AC
Publication year: 2002
Journal: Acta Crystallographica Section D: Biological Crystallography
Journal name in source: Acta crystallographica. Section D, Biological crystallography
Journal acronym: Acta Crystallogr D Biol Crystallogr
Volume: 58
Issue: Pt 10 Pt 2
First page : 1851
Last page: 3
Number of pages: 3
ISSN: 0907-4449
DOI: https://doi.org/10.1107/S0907444902012970(external)
Abstract
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.
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.
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