Syracuse

Backbone assignment of crystalline E. coli maltose binding protein

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Schubeis, Tobias | Stanek, Jan | Pintacuda, Guido

Edité par CCSD ; Springer -

International audience. The E.coli maltose binding protein (MBP) is a 42.5 kDa molecule widely employed in many biotechnology applications. Because of its molecular size, it has become the main model system for the development of solution NMR methods adapted to large biomolecular targets. Here, we report virtually complete (~90%) backbone resonance assignments obtained on a microcrystalline sample of MBP with 1 H-detected solidstate NMR at fast (>100 kHz) magic-angle spinning. We additionally present the detailed description of the methodology employed for the preparation of the sample and the acquisition and analysis of the NMR spectra. The chemical shifts, obtained with a single uniformly 15 N, 13 C-labelled and fully-protonated sample and about two weeks on a 800 MHz NMR spectrometer, have been deposited to the BMRB under the accession number 50089.

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