659 research outputs found

    Implementation and performance of SIBYLS: a dual endstation small-angle X-ray scattering and macromolecular crystallography beamline at the Advanced Light Source.

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    The SIBYLS beamline (12.3.1) of the Advanced Light Source at Lawrence Berkeley National Laboratory, supported by the US Department of Energy and the National Institutes of Health, is optimized for both small-angle X-ray scattering (SAXS) and macromolecular crystallography (MX), making it unique among the world's mostly SAXS or MX dedicated beamlines. Since SIBYLS was commissioned, assessments of the limitations and advantages of a combined SAXS and MX beamline have suggested new strategies for integration and optimal data collection methods and have led to additional hardware and software enhancements. Features described include a dual mode monochromator [containing both Si(111) crystals and Mo/B(4)C multilayer elements], rapid beamline optics conversion between SAXS and MX modes, active beam stabilization, sample-loading robotics, and mail-in and remote data collection. These features allow users to gain valuable insights from both dynamic solution scattering and high-resolution atomic diffraction experiments performed at a single synchrotron beamline. Key practical issues considered for data collection and analysis include radiation damage, structural ensembles, alternative conformers and flexibility. SIBYLS develops and applies efficient combined MX and SAXS methods that deliver high-impact results by providing robust cost-effective routes to connect structures to biology and by performing experiments that aid beamline designs for next generation light sources

    Small-angle X-ray Scattering Studies of the Oligomeric State and Quaternary Structure of the Trifunctional Proline Utilization A (PutA) Flavoprotein from \u3ci\u3eEscherichia coli\u3c/i\u3e

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    Background: Trifunctional proline utilization A (PutA) proteins are multifunctional flavoproteins that catalyze two reactions and repress transcription of the put regulon. Results: PutA from Escherichia coli is a V-shaped dimer, with the DNA-binding domain mediating dimerization. Conclusion: Oligomeric state and quaternary structures are not conserved by PutAs. Significance: The first three-dimensional structural information for any trifunctional PutA is reported

    Small-angle X-ray Scattering Studies of the Oligomeric State and Quaternary Structure of the Trifunctional Proline Utilization A (PutA) Flavoprotein from \u3ci\u3eEscherichia coli\u3c/i\u3e

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    Background: Trifunctional proline utilization A (PutA) proteins are multifunctional flavoproteins that catalyze two reactions and repress transcription of the put regulon. Results: PutA from Escherichia coli is a V-shaped dimer, with the DNA-binding domain mediating dimerization. Conclusion: Oligomeric state and quaternary structures are not conserved by PutAs. Significance: The first three-dimensional structural information for any trifunctional PutA is reported

    Exclusive measurement of coherent eta photoproduction from the deuteron

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    Coherent photoproduction of eta mesons from the deuteron has been measured from threshold up to incident photon energies of 750 MeV using the photon spectrometer TAPS at the tagged photon facility at the Mainz microtron MAMI. For the first time, differential coherent cross sections have been deduced from the coincident detection of the eta meson and the recoil deuteron. A missing energy analysis was used for the suppression of background events so that a very clean identification of coherent eta-photoproduction was achieved. The resulting cross sections agree with previous experimental results except for angles around 90 deg in the photon-deuteron cm-system where they are smaller. They are compared to various model calculations.Comment: 4 pages, 4 figure

    Molecular basis for SMC rod formation and its dissolution upon DNA binding.

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    SMC condensin complexes are central modulators of chromosome superstructure in all branches of life. Their SMC subunits form a long intramolecular coiled coil, which connects a constitutive "hinge" dimerization domain with an ATP-regulated "head" dimerization module. Here, we address the structural arrangement of the long coiled coils in SMC complexes. We unequivocally show that prokaryotic Smc-ScpAB, eukaryotic condensin, and possibly also cohesin form rod-like structures, with their coiled coils being closely juxtaposed and accurately anchored to the hinge. Upon ATP-induced binding of DNA to the hinge, however, Smc switches to a more open configuration. Our data suggest that a long-distance structural transition is transmitted from the Smc head domains to regulate Smc-ScpAB's association with DNA. These findings uncover a conserved architectural theme in SMC complexes, provide a mechanistic basis for Smc's dynamic engagement with chromosomes, and offer a molecular explanation for defects in Cornelia de Lange syndrome
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