Backbone assignment of crystalline E. coli maltose binding protein.

Abstract

The E.coli maltose binding protein (MBP) is a 42.5kDa 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 1H-detected solid-state NMR at fast (> 100kHz) 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 15N,13C-labelled and fully-protonated sample and about 2 weeks on a 800MHz NMR spectrometer, have been deposited to the BMRB under the accession number 50089.