Imaging of Fluorescence Emission from Plant Tissues is presented by Zuzana Benediktyová and Ladislav Nedbal. Exploring Photosynthesis by Electron Tomography is reviewed by Martin F. Hohmann-Marriott and Robert W. Robertson; it summarizes its application to resolve ultrastructures of photosynthetic click here organisms within a few nanometers. Single Particle Electron Microscopy is presented by Egbert J. Boekema, Mihaela Folea, and Roman Kouřil. Simon Scheuring and James N. Stugis provide rationale for imaging, at high resolution, of a native photosynthetic membrane by Atomic Force Microscopy (AFM) to study supramolecular

assembly of the photosynthetic complexes; Scheuring and Stugis show that AFM bridges the resolution gap between atomic structures selleck kinase inhibitor and cellular ultrastructures. MRI is a non-destructive and non-invasive technique that can be used to study the dynamics of plant water relations and water transport. Henk van As, Tom Scheenen, and Frank J. Vergeldt provide an account of MRI techniques that can be used to study plant performance in relation to its photosynthetic activity. Structural methods can be divided into two: (1) for determining

geometric structures and (2) for revealing electronic structures. For understanding how electrons are transferred within an electron transfer chain, or how chemical bonds, which are made up by electrons, are split and rearranged, information on both geometric and electronic structures are equally important for understanding the underlying design principles of unique photosynthetic catalysts. Mei Li and Wen-rui Chang, as well as James P. Allen, Chenda Seng, and Chadwick Larson describe, in two separate contributions, the basics of Protein Crystallography and X-ray Diffraction. Depending on the resolution, this approach can give very detailed information on the geometric structure of the proteins, their cofactors,

and sometimes of bound substrates or products; “snapshots” are taken on deep frozen crystalline samples and provide the structural basis for understanding how proteins function. Junko Yano and Vittal Yachandra describe how X-ray Spectroscopy can be employed to obtain high-resolution data of metal–metal STK38 and metal–ligand distances in active sites of proteins without the need for crystallization of the protein. This technique and the related X-ray Fluorescence method described by Uwe Bergmann and Pieter Glatzel provide important information on the electronic structures of (metal) cofactors. While these X-ray spectroscopy experiments are currently mostly performed with samples frozen in different intermediate states of the catalytic cycle, kinetic X-ray spectroscopy experiments at room temperature can also be performed; these experiments have started to give important information on dynamic changes at (metal) cofactor sites.