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      XFEL data analysis for structural biology

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      Quantitative Biology
      Springer Nature

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          The molecular architecture of the nuclear pore complex.

          Nuclear pore complexes (NPCs) are proteinaceous assemblies of approximately 50 MDa that selectively transport cargoes across the nuclear envelope. To determine the molecular architecture of the yeast NPC, we collected a diverse set of biophysical and proteomic data, and developed a method for using these data to localize the NPC's 456 constituent proteins (see the accompanying paper). Our structure reveals that half of the NPC is made up of a core scaffold, which is structurally analogous to vesicle-coating complexes. This scaffold forms an interlaced network that coats the entire curved surface of the nuclear envelope membrane within which the NPC is embedded. The selective barrier for transport is formed by large numbers of proteins with disordered regions that line the inner face of the scaffold. The NPC consists of only a few structural modules that resemble each other in terms of the configuration of their homologous constituents, the most striking of these being a 16-fold repetition of 'columns'. These findings provide clues to the evolutionary origins of the NPC.
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            Time-resolved serial crystallography captures high-resolution intermediates of photoactive yellow protein.

            Serial femtosecond crystallography using ultrashort pulses from x-ray free electron lasers (XFELs) enables studies of the light-triggered dynamics of biomolecules. We used microcrystals of photoactive yellow protein (a bacterial blue light photoreceptor) as a model system and obtained high-resolution, time-resolved difference electron density maps of excellent quality with strong features; these allowed the determination of structures of reaction intermediates to a resolution of 1.6 angstroms. Our results open the way to the study of reversible and nonreversible biological reactions on time scales as short as femtoseconds under conditions that maximize the extent of reaction initiation throughout the crystal.
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              CrystFEL: a software suite for snapshot serial crystallography

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                Author and article information

                Journal
                Quantitative Biology
                Quant Biol
                Springer Nature
                2095-4689
                2095-4697
                September 2016
                September 2016
                : 4
                : 3
                : 159-176
                Article
                10.1007/s40484-016-0076-z
                4816a908-4def-4a9a-9cc2-04cece74f405
                © 2016
                History

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