Neutron and X-ray analysis of the Fenna – Matthews – Olson photosynthetic antenna complex from Prosthecochloris aestuarii

The Fenna – Matthews – Olson protein from Prosthecochloris aestuarii (PaFMO) has been crystallized in a new form that is amenable to high-resolution X-ray and neutron analysis. The crystals belonged to space group H3, with unit-cell parameters a = b = 83.64, c = 294.78   Å , and diffracted X-rays to ∼ 1.7   Å resolution at room temperature. Large PaFMO crystals grown to volumes of 0.3 – 0.5   mm3 diffracted neutrons to 2.2   Å resolution on the MaNDi neutron diffractometer at the Spallation Neutron Source. The resolution of the neutron data will allow direct determination of the positions of H atoms in the structure, which are believed to be fundamentally important in tuning the individual excitation energies of bacteriochlorophylls in this archetypal photosynthetic antenna complex. This is one of the largest unit-cell systems yet studied using neutron diffraction, and will allow the first high-resolution neutron analysis of a photosynthetic antenna complex.
Source: Acta Crystallographica Section F - Category: Biochemistry Authors: Tags: neutron crystallography photosynthesis hydrogen site energy neutron diffraction Fenna – Matthews Olson protein Prosthecochloris aestuarii research communications Source Type: research
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