April proved to be an eventful month for EU BON, hosting the presentation of two major project results, not only within the same month, but in the course of one week. While CSIC and partners were launching the beta-version of the long-waited Biodiversity Portal in Seville, another EU BON team was busy to search for Integrated approaches for focused biodiversity data mobilization in Stockholm.

About the Portal:

In a dedicated session at the WP2 meeting in Seville, Spain, EU BON partners had the chance to view their work for the last couple of years materialising into one of the main expected project results - the European Biodiversity Portal. That said, what was then presented on 29 April is a beta version, with the final release of the portal planned to become available in early 2017.

Participants at the Seville Workshop, April 2016. Credit: A. Hoffmann

Nonetheless, this beta version already addresses the main aim to offer a unique service for analysing and understanding biodiversity change in Europe. For instance, users can explore how relative abundance of species (within a larger group) changes over time by using big data mediated by GBIF. There is also a spatial browser for locating datasets in any part of the world, which may be usable for computing the EBVs for species populations.

Additionally, an online analytical data processing (OLAP) toolbox has been included in this release. Based on GEOSS technology, the new portal lets users harvest and simultaneously access data from several directories, including GBIF, LTER, EuMon (coming), PESI, and GEOSS sources.

This release also highlights the products of the EU BON project, including new methods and analyses packed in factsheets and infographics for the convenience of scientists and policy users alike. Explore the portal’s beta version here.

Suggestions of how to develop the beta portal further towards the full release are appreciated. Use the feedback form at the welcome page.

Integrated biodiversity data mobilization:

It is a challenge for Bioinformatics group in Europe and around the world to find better ways to integrate different systems and technology. In EU BON’s Task 1.4 the approach to solving this issue was to integrate different systems managing natural history collections and molecular data systems using the best techniques available.

In a dedicated workshop, which took place in Stockholm, Sweden, developers in the sphere of bioinformatics were presented with the project’s Data Mobilization Toolkit. This particular workshop was mainly focused on Docker as a tool to move towards a more integrated environment. Docker has revolutionized system integration and in the workshop the Swedish team shared their experience with dockerizing the DINA-system.

Discussions during the Stockholm workshop; Credit: Karin Karlsson

The workshop ended with a hackathon where they together explored the possibilities for using Docker in selected parts of integrating Pluto-F, JACQ and DINA.

The international Conference will explore the potential of earth observations and thrust climate information transfer from the science to the stakeholder application realm, in order to develop suitable adaptation measures at national and regional levels. It will identify best adaptation programs and approaches to global environmental change in Mediterranean-climate cities. It will enhance and strengthen European and international cooperation in the context of the activities within the Group on Earth Observations (GEO), and promote tools and options for adaptation strategies. The Conference will help local and regional authorities and stakeholders to gain insight on the role of EO-based services in adapting to climate chance impacts in urban hot- spot areas. The Conference will be followed for one and a half day by the 8th GEO European Project Workshop which will be the opportunity to present concrete examples of Earth Observation activities relevant to adaptation strategies.

Information and registration: www.mariolopoulosfoundation.gr/medcity2014

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Deflectometric profilometers are used to precisely measure the form of beam shaping optics of synchrotrons and X-ray free-electron lasers. They often utilize autocollimators which measure slope by evaluating the displacement of a reticle image on a detector. Based on our privileged access to the raw image data of an autocollimator, novel strategies to reduce the systematic measurement errors by using a set of overlapping images of the reticle obtained at different positions on the detector are discussed. It is demonstrated that imaging properties such as, for example, geometrical distortions and vignetting, can be extracted from this redundant set of images without recourse to external calibration facilities. This approach is based on the fact that the properties of the reticle itself do not change – all changes in the reticle image are due to the imaging process. Firstly, by combining interpolation and correlation, it is possible to determine the shift of a reticle image relative to a reference image with minimal error propagation. Secondly, the intensity of the reticle image is analysed as a function of its position on the CCD and a vignetting correction is calculated. Thirdly, the size of the reticle image is analysed as a function of its position and an imaging distortion correction is derived. It is demonstrated that, for different measurement ranges and aperture diameters of the autocollimator, reductions in the systematic errors of up to a factor of four to five can be achieved without recourse to external measurements.

For cryo-electron tomography (cryo-ET) of beam-sensitive biological specimens, a planar sample geometry is typically used. As the sample is tilted, the effective thickness of the sample along the direction of the electron beam increases and the signal-to-noise ratio concomitantly decreases, limiting the transfer of information at high tilt angles. In addition, the tilt range where data can be collected is limited by a combination of various sample-environment constraints, including the limited space in the objective lens pole piece and the possible use of fixed conductive braids to cool the specimen. Consequently, most tilt series are limited to a maximum of ±70°, leading to the presence of a missing wedge in Fourier space. The acquisition of cryo-ET data without a missing wedge, for example using a cylindrical sample geometry, is hence attractive for volumetric analysis of low-symmetry structures such as organelles or vesicles, lysis events, pore formation or filaments for which the missing information cannot be compensated by averaging techniques. Irrespective of the geometry, electron-beam damage to the specimen is an issue and the first images acquired will transfer more high-resolution information than those acquired last. There is also an inherent trade-off between higher sampling in Fourier space and avoiding beam damage to the sample. Finally, the necessity of using a sufficient electron fluence to align the tilt images means that this fluence needs to be fractionated across a small number of images; therefore, the order of data acquisition is also a factor to consider. Here, an n-helix tilt scheme is described and simulated which uses overlapping and interleaved tilt series to maximize the use of a pillar geometry, allowing the entire pillar volume to be reconstructed as a single unit. Three related tilt schemes are also evaluated that extend the continuous and classic dose-symmetric tilt schemes for cryo-ET to pillar samples to enable the collection of isotropic information across all spatial frequencies. A fourfold dose-symmetric scheme is proposed which provides a practical compromise between uniform information transfer and complexity of data acquisition.

A key prerequisite for the successful application of protein crystallography in drug discovery is to establish a robust crystallization system for a new drug-target protein fast enough to deliver crystal structures when the first inhibitors have been identified in the hit-finding campaign or, at the latest, in the subsequent hit-to-lead process. The first crucial step towards generating well folded proteins with a high likelihood of crystallizing is the identification of suitable truncation variants of the target protein. In some cases an optimal length variant alone is not sufficient to support crystallization and additional surface mutations need to be introduced to obtain suitable crystals. In this contribution, four case studies are presented in which rationally designed surface modifications were key to establishing crystallization conditions for the target proteins (the protein kinases Aurora-C, IRAK4 and BUB1, and the KRAS–SOS1 complex). The design process which led to well diffracting crystals is described and the crystal packing is analysed to understand retrospectively how the specific surface mutations promoted successful crystallization. The presented design approaches are routinely used in our team to support the establishment of robust crystallization systems which enable structure-guided inhibitor optimization for hit-to-lead and lead-optimization projects in pharmaceutical research.

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