Expression, purification, crystallization and preliminary X-ray diffraction results from Campylobacter jejuni ferritin

• Published in: Acta crystallographica. Section D, Biological crystallography. Vol. 55; no. 1; pp. 299 - 301
• Main Authors: Clerté, S., Dautant, A., Langlois d'Estaintot, B., Gallois, B., Mizunoe, Y., Wai, S. N., Précigoux, G.
• Format: Journal Article
• Language: English
• Published: 5 Abbey Square, Chester, Cheshire CH1 2HU, England International Union of Crystallography 01-01-1999
• Subjects: Campylobacter jejuni - chemistry; Campylobacter jejuni - genetics; Crystallization; Crystallography, X-Ray; Escherichia coli - genetics; ferritin (C. jejuni); Ferritins - chemistry; Ferritins - genetics; Ferritins - isolation & purification; Gene Expression; Genes, Bacterial; Recombinant Proteins - chemistry; Recombinant Proteins - genetics; Recombinant Proteins - isolation & purification
• ISSN: 1399-0047; 0907-4449; 1399-0047
• DOI: 10.1107/S090744499801004X

The prokaryotic ferritin gene of Campylobacter jejuni was overexpressed in Escherichia coli under control of the bacteriophage T7 promoter and the protein (Cj‐FTN) purified. Preliminary crystallization experiments have been performed using the hanging‐drop vapour‐diffusion method with ammonium sulfate as the precipitant. Diffraction studies show the crystals belong to the I432 space group (a = 151.52 Å). Structure solution by molecular replacement is in progress while crystal quality improvement is carried out.