Agroforesterie et services écosystémiques en zone tropicale

Respectueux de l’environnement et garantissant une sécurité alimentaire soutenue par la diversification des productions et des revenus qu’ils procurent, les systèmes agroforestiers apparaissent comme un modèle prometteur d’agriculture durable dans les pays du Sud les plus vulnérables aux changements globaux. Cependant, ces systèmes agroforestiers ne peuvent être optimisés qu’à condition de mieux comprendre et de mieux maîtriser les facteurs de leurs productions. L’ouvrage présente un ensemble de connaissances récentes sur les mécanismes biophysiques et socio-économiques qui sous-tendent le fonctionnement et la dynamique des systèmes agroforestiers. Il concerne, d’une part les systèmes agroforestiers à base de cultures pérennes, telles que cacaoyers et caféiers, de régions tropicales humides en Amérique du Sud, en Afrique de l’Est et du Centre, d’autre part les parcs arborés et arbustifs à base de cultures vivrières, principalement de céréales, de la région semi-aride subsaharienne d’Afrique de l’Ouest. Il synthétise les dernières avancées acquises grâce à plusieurs projets associant le Cirad, l’IRD et leurs partenaires du Sud qui ont été conduits entre 2012 et 2016 dans ces régions. L’ensemble de ces projets s’articulent autour des dynamiques des systèmes agroforestiers et des compromis entre les services de production et les autres services socio-écosystémiques que ces systèmes fournissent

Adding Size Exclusion Chromatography (SEC) and Light Scattering (LS) Devices to Obtain High-Quality Small Angle X-Ray Scattering (SAXS) Data

We describe the updated size-exclusion chromatography small angle X-ray scattering (SEC-SAXS) set-up used at the P12 bioSAXS beam line of the European Molecular Biology Laboratory (EMBL) at the PETRAIII synchrotron, DESY Hamburg (Germany). The addition of size exclusion chromatography (SEC) directly on-line to the SAXS capillary has become a well-established approach to reduce the effects of the sample heterogeneity on the SAXS measurements. The additional use of multi-angle laser light scattering (MALLS), UV absorption spectroscopy, refractive index (RI), and quasi-elastic light scattering (QELS) in parallel to the SAXS measurements enables independent molecular weight validation and hydrodynamic radius estimates. This allows one to address sample monodispersity as well as conformational heterogeneity. The benefits of the current SEC-SAXS set-up are demonstrated on a set of selected standard proteins. The processed SEC-SAXS data and models are provided in the Small Angle Scattering Biological Data Bank (SASBDB) and are labeled as “bench-marked” datasets that include the unsubtracted data frames spanning the respective SEC elution profiles and corresponding MALLS-UV-RI-QELS data. These entries provide method developers with datasets suitable for testing purposes, in addition to an educational resource for SAS data analysis and modeling

Rapid screening of in cellulo grown protein crystals via a small-angle X-ray scattering/X-ray powder diffraction synergistic approach

Crystallization of recombinant proteins in living cells is an exciting new approach for structural biology that provides an alternative to the time-consuming optimization of protein purification and extensive crystal screening steps. Exploiting the potential of this approach requires a more detailed understanding of the cellular processes involved and versatile screening strategies for crystals in a cell culture. Particularly if the target protein forms crystalline structures of unknown morphology only in a small fraction of cells, their detection by applying standard visualization techniques can be time consuming and difficult owing to the environmental challenges imposed by the living cells. In this study, a high-brilliance and low-background bioSAXS beamline is employed for rapid and sensitive detection of protein microcrystals grown within insect cells. On the basis of the presence of Bragg peaks in the recorded small-angle X-ray scattering profiles, it is possible to assess within seconds whether a cell culture contains microcrystals, even in a small percentage of cells. Since such information cannot be obtained by other established detection methods in this time frame, this screening approach has the potential to overcome one of the bottlenecks of intracellular crystal detection. Moreover, the association of the Bragg peak positions in the scattering curves with the unit-cell composition of the protein crystals raises the possibility of investigating the impact of environmental conditions on the crystal structure of the intracellular protein crystals. This information provides valuable insights helping to further understand the in cellulo crystallization process

Quaternary structure of human, Drosophila melanogaster and Caenorhabditis elegans MFE-2 in solution from synchrotron small-angle X-ray scattering

Multifunctional enzyme type 2 (MFE-2) forms part of the fatty acid b-oxidation pathway in peroxisomes.MFE-2s from various species reveal proteins with structurally homologous functionaldomains assembled in different compilations. Crystal structures of all domain types are known.SAXS data from human, fruit fly and Caenorhabditis elegans MFE-2s and their constituent domainswere collected, and both ab initio and rigid body models constructed. Location of the putative substratebinding helper domain SCP-2L (sterol carrier protein 2-like), which is not part of MFE-2 proteinin every species and not seen as part of any previous MFE-2 structures, was determined. Theobtained models of human and C. elegans MFE-2 lend a direct structural support to the idea ofthe biological role of SCP-2L