Webometric analysis of departments of librarianship and information science: a follow-up study

This paper reports an analysis of the websites of UK departments of library and information science. Inlink counts of these websites revealed no statistically significant correlation with the quality of the research carried out by these departments, as quantified using departmental grades in the 2001 Research Assessment Exercise and citations in Google Scholar to publications submitted for that Exercise. Reasons for this lack of correlation include: difficulties in disambiguating departmental websites from larger institutional structures; the relatively small amount of research-related material in departmental websites; and limitations in the ways that current Web search engines process linkages to URLs. It is concluded that departmental-level webometric analyses do not at present provide an appropriate technique for evaluating academic research quality, and, more generally, that standards are needed for the formatting of URLs if inlinks are to become firmly established as a tool for website analysis

Impact Factor: outdated artefact or stepping-stone to journal certification?

A review of Garfield's journal impact factor and its specific implementation as the Thomson Reuters Impact Factor reveals several weaknesses in this commonly-used indicator of journal standing. Key limitations include the mismatch between citing and cited documents, the deceptive display of three decimals that belies the real precision, and the absence of confidence intervals. These are minor issues that are easily amended and should be corrected, but more substantive improvements are needed. There are indications that the scientific community seeks and needs better certification of journal procedures to improve the quality of published science. Comprehensive certification of editorial and review procedures could help ensure adequate procedures to detect duplicate and fraudulent submissions.Comment: 25 pages, 12 figures, 6 table

Combined 1H-Detected solid-state NMR spectroscopy and electron cryotomography to study membrane proteins across resolutions in native environments

Membrane proteins remain challenging targets for structural biology, despite much effort, as their native environment is heterogeneous and complex. Most methods rely on detergents to extract membrane proteins from their native environment, but this removal can significantly alter the structure and function of these proteins. Here, we overcome these challenges with a hybrid method to study membrane proteins in their native membranes, combining high-resolution solid-state nuclear magnetic resonance spectroscopy and electron cryotomography using the same sample. Our method allows the structure and function of membrane proteins to be studied in their native environments, across different spatial and temporal resolutions, and the combination is more powerful than each technique individually. We use the method to demonstrate that the bacterial membrane protein YidC adopts a different conformation in native membranes and that substrate binding to YidC in these native membranes differs from purified and reconstituted system