6MEZ
X-ray structure of the Fenna-Matthews-Olsen antenna complex from Prosthecochloris aestuarii
Summary for 6MEZ
Entry DOI | 10.2210/pdb6mez/pdb |
Related | 6E9J |
Descriptor | Bacteriochlorophyll a protein, BACTERIOCHLOROPHYLL A, SULFATE ION, ... (4 entities in total) |
Functional Keywords | fmo photosynthesis antenna complex, energy transfer, photosynthesis |
Biological source | Prosthecochloris aestuarii |
Total number of polymer chains | 2 |
Total formula weight | 92664.28 |
Authors | Selvaraj, B.,Lu, X.,Cuneo, M.J.,Myles, D.A.A. (deposition date: 2018-09-07, release date: 2019-03-13, Last modification date: 2024-03-13) |
Primary citation | Lu, X.,Selvaraj, B.,Ghimire-Rijal, S.,Orf, G.S.,Meilleur, F.,Blankenship, R.E.,Cuneo, M.J.,Myles, D.A.A. Neutron and X-ray analysis of the Fenna-Matthews-Olson photosynthetic antenna complex from Prosthecochloris aestuarii. Acta Crystallogr F Struct Biol Commun, 75:171-175, 2019 Cited by PubMed Abstract: 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 mm 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. PubMed: 30839291DOI: 10.1107/S2053230X19000724 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.74 Å) |
Structure validation
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