Isolation, crystallization, and investigation of ribosomal protein S8 complexed with specific fragments of rRNA of bacterial or archaeal origin. Biochemistry 66

Study of the nature of protein-rRNA complexes is a topical problem of modern molecular biology. Structural studies of rRNA-protein complexes are the most direct and precise method of analysis of these interactions. Because ribosomal proteins are most conservative during evolution, their complexes with specific RNA fragments provide an interesting model for studying RNA-protein interactions. Ribosomal protein S8 from E. coli plays a key role in assembling the small ribosomal subunit The major region of protein S8 binding on 16S rRNA was determined by partial hydrolysis with restric tion endonucleases The binding sites of protein S8 on 16S rRNA are similar in E. coli and T. thermophilus. It was shown that ACCELERATED PUBLICATION 0006 2979/01/6609 0948$25.00 ©2001 MAIK "Nauka / Interperiodica" * To whom correspondence should be addressed. Vol. 66, No. 9, 2001, pp. 948 953. Translated from Biokhimiya, Vol. 66, No. 9, 2001, pp. 1165 1171. Original Russian Text Copyright © 2001 Abstract-The core ribosomal protein S8 binds to the central domain of 16S rRNA independently of other ribosomal proteins and is required for assembling the 30S subunit. It has been shown with E. coli ribosomes that a short rRNA fragment restrict ed by nucleotides 588 602 and 636 651 is sufficient for strong and specific protein S8 binding. In this work, we studied the complexes formed by ribosomal protein S8 from Thermus thermophilus and Methanococcus jannaschii with short rRNA frag ments isolated from the same organisms. The dissociation constants of the complexes of protein S8 with rRNA fragments were determined. Based on the results of binding experiments, rRNA fragments of different length were designed and syn thesized in preparative amounts in vitro using T7 RNA polymerase. Stable S8-RNA complexes were crystallized. Crystals were obtained both for homologous bacterial and archaeal complexes and for hybrid complexes of archaeal protein with bac terial rRNA. Crystals of the complex of protein S8 from M. jannaschii with the 37 nucleotide rRNA fragment from the same organism suitable for X ray analysis were obtained

#EEGManyLabs: Investigating the Replicability of Influential EEG Experiments

There is growing awareness across the neuroscience community that the replicability of findings about the relationship between brain activity and cognitive phenomena can be improved by conducting studies with high statistical power that adhere to well-defined and standardised analysis pipelines. Inspired by recent efforts from the psychological sciences, and with the desire to examine some of the foundational findings using electroencephalography (EEG), we have launched #EEGManyLabs, a large-scale international collaborative replication effort. Since its discovery in the early 20th century, EEG has had a profound influence on our understanding of human cognition, but there is limited evidence on the replicability of some of the most highly cited discoveries. After a systematic search and selection process, we have identified 27 of the most influential and continually cited studies in the field. We plan to directly test the replicability of key findings from 20 of these studies in teams of at least three independent laboratories. The design and protocol of each replication effort will be submitted as a Registered Report and peer-reviewed prior to data collection. Prediction markets, open to all EEG researchers, will be used as a forecasting tool to examine which findings the community expects to replicate. This project will update our confidence in some of the most influential EEG findings and generate a large open access database that can be used to inform future research practices. Finally, through this international effort, we hope to create a cultural shift towards inclusive, high-powered multi-laboratory collaborations. © 2021 The Authors

Nursery vouchers in Wales A detailed guide - update

English/Welsh text on inverted pagesAvailable from British Library Document Supply Centre-DSC:GPE/0227 / BLDSC - British Library Document Supply CentreSIGLEGBUnited Kingdo

Stratigraphic evidence for an early Holocene earthquake in Aceh, Indonesia

The Holocene stratigraphy of the coastal plain of the Aceh Province of Sumatra contains 6 m of sediment with three regionally consistent buried soils above pre-Quaternary bedrock or pre-Holocene unconsolidated sediment. Litho-, bio-, and chronostratigraphic analyses of the lower buried soil reveals a rapid change in relative sea-level caused by coseismic subsidence during an early Holocene megathrust earthquake. Evidence for paleoseismic subsidence is preserved as a buried mangrove soil, dominated by a pollen assemblage of Rhizophora and/or Bruguiera/Ceriops taxa. The soil is abruptly overlain by a thin tsunami sand. The sand contains mixed pollen and abraded foraminiferal assemblages of both offshore and onshore environments. The tsunami sand grades upward into mud that contains both well-preserved foraminifera of intertidal origin and individuals of the gastropod Cerithidea cingulata. Radiocarbon ages from the pre- and post-seismic sedimentary sequences constrain the paleoearthquake to 6500–7000 cal. yrs. BP. We use micro-and macrofossil data to determine the local paleoenvironment before and after the earthquake. We estimate coseismic subsidence to be 0.45 ± 0.30 m, which is comparable to the 0.6 m of subsidence observed during the 2004 Aceh–Andaman earthquake on Aceh’s west coast