Structural highlights
FunctionBCPA_PROAE Intermediary in the transfer of excitation energy from the chlorophyll to the reaction centers. Publication Abstract from PubMedThe 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 A, and diffracted X-rays to approximately 1.7 A resolution at room temperature. Large PaFMO crystals grown to volumes of 0.3-0.5 mm(3) diffracted neutrons to 2.2 A 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. Neutron and X-ray analysis of the Fenna-Matthews-Olson photosynthetic antenna complex from Prosthecochloris aestuarii.,Lu X, Selvaraj B, Ghimire-Rijal S, Orf GS, Meilleur F, Blankenship RE, Cuneo MJ, Myles DAA Acta Crystallogr F Struct Biol Commun. 2019 Mar 1;75(Pt 3):171-175. doi:, 10.1107/S2053230X19000724. Epub 2019 Feb 20. PMID:30839291[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
| ||||||||||||||||||||
This page was last modified 13:29, 13 August 2026.