We present the results for CAPRI Round 30, the first joint CASP-CAPRI experiment, which brought together experts from the protein structure prediction and protein-protein docking communities. The Round comprised 25 targets from amongst those submitted for the CASP11 prediction experiment of 2014. The targets included mostly homodimers, a few homotetramers, and two heterodimers, and comprised protein chains that could readily be modeled using templates from the Protein Data Bank. On average 24 CAPRI groups and 7 CASP groups submitted docking predictions for each target, and 12 CAPRI groups per target participated in the CAPRI scoring experiment. In total more than 9500 models were assessed against the 3D structures of the corresponding target complexes. Results show that the prediction of homodimer assemblies by homology modeling techniques and docking calculations is quite successful for targets featuring large enough subunit interfaces to represent stable associations. Targets with ambiguous or inaccurate oligomeric state assignments, often featuring crystal contact-sized interfaces, represented a confounding factor. For those, a much poorer prediction performance was achieved, while nonetheless often providing helpful clues on the correct oligomeric state of the protein. The prediction performance was very poor for genuine tetrameric targets, where the inaccuracy of the homology-built subunit models and the smaller pair-wise interfaces severely limited the ability to derive the correct assembly mode. Our analysis also shows that docking procedures tend to perform better than standard homology modeling techniques and that highly accurate models of the protein components are not always required to identify their association modes with acceptable accuracy.

The second generation Antarctic magnetic anomaly compilation for the region south of 60°S includes some 3.5 million line-km of aeromagnetic and marine magnetic data that more than doubles the initial map's near-surface database. For the new compilation, the magnetic data sets were corrected for the International Geomagnetic Reference Field, diurnal effects, and high-frequency errors and leveled, gridded, and stitched together. The new magnetic data further constrain the crustal architecture and geological evolution of the Antarctic Peninsula and the West Antarctic Rift System in West Antarctica, as well as Dronning Maud Land, the Gamburtsev Subglacial Mountains, the Prince Charles Mountains, Princess Elizabeth Land, and Wilkes Land in East Antarctica and the circumjacent oceanic margins. Overall, the magnetic anomaly compilation helps unify disparate regional geologic and geophysical studies by providing new constraints on major tectonic and magmatic processes that affected the Antarctic from Precambrian to Cenozoic times.Plain Language Summary Given the ubiquitous polar cover of snow, ice, and seawater, the magnetic anomaly compilation offers important constraints on the global tectonic processes and crustal properties of the Antarctic. It also links widely separated areas of outcrop to help unify disparate geologic studies and provides insights on the lithospheric transition between Antarctica and adjacent oceans, as well as the geodynamic evolution of the Antarctic lithosphere in the assembly and breakup of the Gondwana, Rodinia, and Columbia supercontinents and key piercing points for reconstructing linkages between the protocontinents. The magnetic data together with ice-probing radar and gravity information greatly facilitate understanding the evolution of fundamental large-scale geological processes such as continental rifting, intraplate mountain building, subduction and terrane accretion processes, and intraplate basin formation.

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Cellulose microfibrils are para-crystalline arrays of several dozen linear (1→4)-β-d-glucan chains synthesized at the surface of the cell membrane by large, multimeric complexes of synthase proteins. Recombinant catalytic domains of rice (Oryza sativa) CesA8 cellulose synthase form dimers reversibly as the fundamental scaffold units of architecture in the synthase complex. Specificity of binding to UDP and UDP-Glc indicates a properly folded protein, and binding kinetics indicate that each monomer independently synthesizes single glucan chains of cellulose, i.e., two chains per dimer pair. In contrast to structure modeling predictions, solution x-ray scattering studies demonstrate that the monomer is a two-domain, elongated structure, with the smaller domain coupling two monomers into a dimer. The catalytic core of the monomer is accommodated only near its center, with the plant-specific sequences occupying the small domain and an extension distal to the catalytic domain. This configuration is in stark contrast to the domain organization obtained in predicted structures of plant CesA. The arrangement of the catalytic domain within the CesA monomer and dimer provides a foundation for constructing structural models of the synthase complex and defining the relationship between the rosette structure and the cellulose microfibrils they synthesize.

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