Article Metrics


Online attention

A putative siderophore-interacting protein from the marine bacterium Shewanella frigidimarina NCIMB 400: cloning, expression, purification, crystallization and X-ray diffraction analysis

DOI: 10.1107/S2053230X16011419 DOI Help

Authors: Inês B. Trindade (Institudo Tecnologia Quimica e Biologica) , Bruno M. Fonseca (Institudo Tecnologia Quimica e Biologica) , Pedro Matias (Institudo Tecnologia Quimica e Biologica) , Ricardo O. Louro (Instituto de Tecnologia Química e Biológica) , Elin Moe (Instituto de Tecnologia Química e Biológica)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Acta Crystallographica Section F Structural Biology Communications , VOL 72

State: Published (Approved)
Published: September 2016
Diamond Proposal Number(s): 10515 , 14707

Open Access Open Access

Abstract: Siderophore-binding proteins (SIPs) perform a key role in iron acquisition in multiple organisms. In the genome of the marine bacterium Shewanella frigidimarina NCIMB 400, the gene tagged as SFRI_RS12295 encodes a protein from this family. Here, the cloning, expression, purification and crystallization of this protein are reported, together with its preliminary X-ray crystallographic analysis to 1.35 Å resolution. The SIP crystals belonged to the monoclinic space group P21, with unit-cell parameters a = 48.04, b = 78.31, c = 67.71 Å, [alpha] = 90, [beta] = 99.94, [gamma] = 90°, and are predicted to contain two molecules per asymmetric unit. Structure determination by molecular replacement and the use of previously determined ~2 Å resolution SIP structures with ~30% sequence identity as templates are ongoing.

Journal Keywords: siderophore-interacting protein; Shewanella frigidimarina; crystallographic analysis

Subject Areas: Biology and Bio-materials, Medicine

Instruments: I04-Macromolecular Crystallography