Partners

Partner 9: CIRMMP, Magnetic Resonance Center, CERM, Florence.

Partner: Professor Ivano Bertini
Deputy: Professor Lucia Banci

The Magnetic Resonance Center of the University of Florence (CERM), managed by the consortium CIRMMP has long-standing experience in structural biology with particular focus on the role of metal ions in cellular processes, investigated through a combination of bioinformatic and NMR methods. It also has expertise in cloning, expression and purification of proteins.
The NMR instrumentation available at CERM comprises high resolution NMR spectrometers with magnetic fields ranging from 200 MHz to 900 MHz. A 700 MHz spectrometer devoted to solid state is also available. All instruments are state-of-the-art digital spectrometers. Each high resolution instrument is equipped with several probes to meet the most disparate experimental conditions. Among them, Cryoprobes for the spectrometer working at 500, 800 and 900 MHz, a prototype TXO probe for 13C-detection at one of the two 700 MHz, and two high power probes for 600 and 800 MHz are available. On the low field end, the laboratory is unique for the efforts devoted to the development of relaxometry: a non commercial Field Cycling Relaxometer, operating in the 0.01-50 MHz range, is available and a newly designed Fast Field Cycling Relaxometer, operating in the 0.001- 80 MHz range. Also available to the team are: bioinformatic tools for genome analysis; molecular Biology labs fully equipped and automated for HTP protein cloning, expression and production with robotic equipment; mass spectrometry (MALDI-TOF and ESI instrumentation); atomic absorption (ICP), W- and X-band EPR and isothermal titration calorimetry (ITC).
The team comprises 10 senior research staff members, coordinating research groups with expertise spanning from browsing of gene databanks to protein expression and structure determination. The team has a unique expertise in NMR of paramagnetic systems, has characterized several metalloproteins, and has developed several unique software tools to include paramagnetism-based restraints in available solution structure calculation protocols and bioinformatics tools for them. CERM has solved, both by NMR and by X-ray, more than 90 protein structures, a large share of which are metalloproteins.