A quality assurance phantom for electronic portal imaging devices

Electronic portal imaging device (EPID) plays an important role in radiation therapy portal imaging, geometric and dosimetric verification. Consistent image quality and stable radiation response is necessary for proper utilization that requires routine quality assurance (QA). A commercial ‘EPID QC’ phantom weighing 3.8 kg with a dimension of 25 × 25 × 4.8 cm3 is used for EPID QA. This device has five essential tools to measure the geometric accuracy, signal‐to‐noise ratio (SNR), dose linearity, and the low‐ and the high‐contrast resolutions. It is aligned with beam divergence to measure the imaging and geometric parameters in both X and Y directions, and can be used as a baseline check for routine QA. The low‐contrast tool consists of a series of holes with various diameters and depths in an aluminum slab, very similar to the Las Vegas phantom. The high‐resolution contrast tool provides the modulation transfer function (MTF) in both the x‐ and y‐dimensions to measure the focal spot of linear accelerator that is important for imaging and small field dosimetry. The device is tested in different institutions with various amorphous silicon imagers including Elekta, Siemens and Varian units. Images of the QA phantom were acquired at 95.2 cm source‐skin‐distance (SSD) in the range 1–15 MU for a 26 × 26 cm2 field and phantom surface is set normal to the beam direction when gantry is at 0° and 90°. The epidSoft is a software program provided with the EPID QA phantom for analysis of the data. The preliminary results using the phantom on the tested EPID showed very good low‐contrast resolution and high resolution, and an MTF (0.5) in the range of 0.3–0.4 lp/mm. All imagers also exhibit satisfactory geometric accuracy, dose linearity and SNR, and are independent of MU and spatial orientations. The epidSoft maintains an image analysis record and provides a graph of the temporal variations in imaging parameters. In conclusion, this device is simple to use and provides testing on basic and advanced imaging parameters for daily QA on any imager used in clinical practice

Light Harvesting by Lamellar Chromatophores in Rhodospirillum photometricum

International audiencePurple photosynthetic bacteria harvest light using pigment-protein complexes which are often arranged in pseudo-organelles called chromatophores. A model of a chromatophore from Rhodospirillum photometricum was constructed based on atomic force microscopy data. Molecular-dynamics simulations and quantum-dynamics calculations were performed to characterize the intercomplex excitation transfer network and explore the interplay between close-packing and light-harvesting efficiency

Membrane Curvature Induced by Aggregates of LH2s and Monomeric LH1s

The photosynthetic apparatus of purple bacteria is contained within organelles called chromatophores, which form as extensions of the cytoplasmic membrane. The shape of these chromatophores can be spherical (as in Rhodobacter sphaeroides), lamellar (as in Rhodopseudomonas acidophila and Phaeospirillum molischianum), or tubular (as in certain Rb. sphaeroides mutants). Chromatophore shape is thought to be influenced by the integral membrane proteins Light Harvesting Complexes I and II (LH1 and LH2), which pack tightly together in the chromatophore. It has been suggested that the shape of LH2, together with its close packing in the membrane, induces membrane curvature. The mechanism of LH2-induced curvature is explored via molecular dynamics simulations of multiple LH2 complexes in a membrane patch. LH2s from three species—Rb. sphaeroides, Rps. acidophila, and Phsp. molischianum—were simulated in different packing arrangements. In each case, the LH2s pack together and tilt with respect to neighboring LH2s in a way that produces an overall curvature. This curvature appears to be driven by a combination of LH2's shape and electrostatic forces that are modulated by the presence of well-conserved cytoplasmic charged residues, the removal of which inhibits LH2 curvature. The interaction of LH2s and an LH1 monomer is also explored, and it suggests that curvature is diminished by the presence of LH1 monomers. The implications of our results for chromatophore shape are discussed

Intrinsic Curvature Properties of Photosynthetic Proteins in Chromatophores

In purple bacteria, photosynthesis is carried out on large indentations of the bacterial plasma membrane termed chromatophores. Acting as primitive organelles, chromatophores are densely packed with the membrane proteins necessary for photosynthesis, including light harvesting complexes LH1 and LH2, reaction center (RC), and cytochrome bc1. The shape of chromatophores is primarily dependent on species, and is typically spherical or flat. How these shapes arise from the protein-protein and protein-membrane interactions is still unknown. Now, using molecular dynamics simulations, we have observed the dynamic curvature of membranes caused by proteins in the chromatophore. A membrane-embedded array of LH2s was found to relax to a curved state, both for LH2 from Rps. acidophila and a homology-modeled LH2 from Rb. sphaeroides. A modeled LH1-RC-PufX dimer was found to develop a bend at the dimerizing interface resulting in a curved shape as well. In contrast, the bc1 complex, which has not been imaged yet in native chromatophores, did not induce a preferred membrane curvature in simulation. Based on these results, a model for how the different photosynthetic proteins influence chromatophore shape is presented

Photosynthetic Vesicle Architecture and Constraints on Efficient Energy Harvesting

Photosynthetic chromatophore vesicles found in some purple bacteria constitute one of the simplest light-harvesting systems in nature. The overall architecture of chromatophore vesicles and the structural integration of vesicle function remain poorly understood despite structural information being available on individual constituent proteins. An all-atom structural model for an entire chromatophore vesicle is presented, which improves upon earlier models by taking into account the stoichiometry of core and antenna complexes determined by the absorption spectrum of intact vesicles in Rhodobacter sphaeroides, as well as the well-established curvature-inducing properties of the dimeric core complex. The absorption spectrum of low-light-adapted vesicles is shown to correspond to a light-harvesting-complex 2 to reaction center ratio of 3:1. A structural model for a vesicle consistent with this stoichiometry is developed and used in the computation of excitonic properties. Considered also is the packing density of antenna and core complexes that is high enough for efficient energy transfer and low enough for quinone diffusion from reaction centers to cytochrome bc1 complexes

Membrane-Bending Mechanism of Amphiphysin N-BAR Domains

BAR domains are highly conserved protein domains participating in a diversity of cellular processes that involve membrane remodeling. The mechanisms underlying such remodeling are debated. For the relatively well-studied case of amphiphysin N-BAR domain, one suggested mechanism involves scaffolding, i.e., binding of a negatively charged membrane to the protein's positively charged curved surface. An alternative mechanism suggests that insertion of the protein's N-terminal amphipathic segments (N-helices H0) into the membrane leads to bending. Here, we address the issue through all-atom and coarse-grained simulations of multiple amphiphysin N-BAR domains and their components interacting with a membrane. We observe that complete N-BAR domains and BAR domains without H0s bend the membrane, but H0s alone do not, which suggests that scaffolding, rather than helix insertion, plays a key role in membrane sculpting by amphiphysin N-BAR domains