Crystallographic MAD Phasing Strategies Explored Using ELETTRA Sincrotrone Mn K-Edge Data to 2.1 Å and Use of CHESS Establishes the Diffraction Resolution Limit as 0.92 Å for the Protein Mn, Ca Concanavalin A

Multiwavelength anomalous dispersion (MAD) data have been collected from a single crystal of the protein concanavalin A so as to evaluate different combinations of wavelengths for crystallographic structure determination. Data were recorded to 2.1 Å resolution on a flash frozen crystal at three wavelengths about the Mn K-edge (1.8951 Å, 1.8940 Å, 1.800 Å) using synchrotron radiation at ELETTRA's Sincrotrone Trieste 'XRD' beamline. This is one of the longest wavelength K-edge MAD studies undertaken to date. Anomalous and dispersive Patterson maps are seen to be of high quality and indicate a high occupancy for the manganese binding site. This is confirmed also in the MAD phase determination and electron density maps. Finally 0.92 Å data recorded at CHESS indicates the prospects available for combined phasing strategies based on MAD to medium/high resolution along with ultra high resolution data.