Microphysical particle properties derived from inversion algorithms developed in the framework of EARLINET

© Author(s) 2015. CC Attribution 3.0 License. An earlier version of this paper was published in Atmospheric Measurement Techniques Discussions: https://dx.doi.org/10.5194/amtd-8-12823-2015.We present a summary on the current status of two inversion algorithms that are used in EARLINET for the inversion of data collected with EARLINET multiwavelength Raman lidars. These instruments measure backscatter coecients at 355, 532, and 1064 nm, and extinction coecients at 355 and 532 nm. Development of these two algorithms started in 2000 when EARLINET was founded. The algorithms are based on manually controlled inversion of optical data which allows for detailed sensitivity studies and thus provides us with comparably high quality of the derived data products. The algorithms allow us to derive particle eective radius, and volume and surface-area concentration with comparably high confidence. The retrieval of the real and imaginary parts of the complex refractive index still is a challenge in view of the accuracy required for these parameters in climate change studies in which light-absorption needs to be known with high accuracy. Single-scattering albedo can be computed from the retrieved microphysical parameters and allows us to categorize aerosols into high and low absorbing aerosols. We discuss the current status of these manually operated algorithms, the potentially achievable accuracy of data products, and the goals for future work on the basis of a few exemplary simulations with synthetic optical data. The optical data used in our study cover a range of Ångström exponents and extinction-to-backscatter (lidar) ratios that are found from lidar measurements of various aerosol types.We also tested aerosol scenarios that are considered highly unlikely, e.g., the lidar ratios fall outside the commonly accepted range of values measured with Raman lidar, even though the underlying microphysical particle properties are not uncommon. The goal of this part of the study is to test robustness of the algorithms toward their ability to identify aerosol types that have not been measured so far, but cannot be ruled out based on our current knowledge of aerosol physics. We computed the optical data from monomodal logarithmic particle size distributions, i.e., we explicitly excluded the more complicated case of bimodal particle size distributions which is a topic of ongoing research work. Another constraint is that we only considered particles of spherical shape in our simulations. We considered particle radii as large as 7–10 μm in our simulations. That particle size does not only cover the size range of particles in the fine-mode fraction of naturally occurring particle size distributions but also covers a considerable part of the coarse-mode fraction of particle size distributions. We considered optical-data errors of 15% in the simulation studies. We target 50% uncertainty as a reasonable threshold for our data products, though we attempt to obtain data products with less uncertainty in future work.Peer reviewe

Drilling operations for the South Pole Ice Core (SPICEcore) project

Over the course of the 2014/15 and 2015/16 austral summer seasons, the South Pole Ice Core project recovered a 1751 m deep ice core at the South Pole. This core provided a high-resolution record of paleoclimate conditions in East Antarctica during the Holocene and late Pleistocene. The drilling and core processing were completed using the new US Intermediate Depth Drill system, which was designed and built by the US Ice Drilling Program at the University of Wisconsin–Madison. In this paper, we present and discuss the setup, operation, and performance of the drill system

SSMap: A new UniProt-PDB mapping resource for the curation of structural-related information in the UniProt/Swiss-Prot Knowledgebase

<p>Abstract</p> <p>Background</p> <p>Sequences and structures provide valuable complementary information on protein features and functions. However, it is not always straightforward for users to gather information concurrently from the sequence and structure levels. The UniProt knowledgebase (UniProtKB) strives to help users on this undertaking by providing complete cross-references to Protein Data Bank (PDB) as well as coherent feature annotation using available structural information. In this study, SSMap – a new UniProt-PDB residue-residue level mapping – was generated. The primary objective of this mapping is not only to facilitate the two tasks mentioned above, but also to palliate a number of shortcomings of existent mappings. SSMap is the first isoform sequence-specific mapping resource and is up-to-date for UniProtKB annotation tasks. The method employed by SSMap differs from the other mapping resources in that it stresses on the correct reconstruction of the PDB sequence from structures, and on the correct attribution of a UniProtKB entry to each PDB chain by using a series of post-processing steps.</p> <p>Results</p> <p>SSMap was compared to other existing mapping resources in terms of the correctness of the attribution of PDB chains to UniProtKB entries, and of the quality of the pairwise alignments supporting the residue-residue mapping. It was found that SSMap shared about 80% of the mappings with other mapping sources. New and alternative mappings proposed by SSMap were mostly good as assessed by manual verification of data subsets. As for local pairwise alignments, it was shown that major discrepancies (both in terms of alignment lengths and boundaries), when present, were often due to differences in methodologies used for the mappings.</p> <p>Conclusion</p> <p>SSMap provides an independent, good quality UniProt-PDB mapping. The systematic comparison conducted in this study allows the further identification of general problems in UniProt-PDB mappings so that both the coverage and the quality of the mappings can be systematically improved for the benefit of the scientific community. SSMap mapping is currently used to provide PDB cross-references in UniProtKB.</p

ArachnoServer 2.0, an updated online resource for spider toxin sequences and structures

ArachnoServer (www.arachnoserver.org) is a manually curated database providing information on the sequence, structure and biological activity of protein toxins from spider venoms. These proteins are of interest to a wide range of biologists due to their diverse applications in medicine, neuroscience, pharmacology, drug discovery and agriculture. ArachnoServer currently manages 1078 protein sequences, 759 nucleic acid sequences and 56 protein structures. Key features of ArachnoServer include a molecular target ontology designed specifically for venom toxins, current and historic taxonomic information and a powerful advanced search interface. The following significant improvements have been implemented in version 2.0: (i) the average and monoisotopic molecular masses of both the reduced and oxidized form of each mature toxin are provided; (ii) the advanced search feature now enables searches on the basis of toxin mass, external database accession numbers and publication date in ArachnoServer; (iii) toxins can now be browsed on the basis of their phyletic specificity; (iv) rapid BLAST searches based on the mature toxin sequence can be performed directly from the toxin card; (v) private silos can be requested from research groups engaged in venoms-based research, enabling them to easily manage and securely store data during the process of toxin discovery; and (vi) a detailed user manual is now available