Macromolecular Crystallography: Deciphering the Structure, - download pdf or read online

By Qian Wu, Lynn Sibanda, Takashi Ochi (auth.), Maria Armenia Carrondo, Paola Spadon (eds.)

ISBN-10: 9400725299

ISBN-13: 9789400725294

ISBN-10: 9400725302

ISBN-13: 9789400725300

This quantity is a suite of the contributions awarded on the forty second Erice Crystallographic direction whose major aim used to be to coach the more youthful iteration on complex tools and methods for reading structural and dynamic facets of organic macromolecules. The papers evaluate the strategies used to review protein assemblies and their dynamics, together with X-ray diffraction and scattering, electron cryo-electron microscopy, electro nanospray mass spectrometry, NMR, protein docking and molecular dynamics.
A key topic through the publication is the dependence of contemporary structural technological know-how on a number of experimental and computational options, and it's the improvement of those suggestions and their integration that may take us ahead within the future.

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Additional info for Macromolecular Crystallography: Deciphering the Structure, Function and Dynamics of Biological Molecules

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O’Driscoll M, Jeggo PA (2005) The role of double-strand break repair — insights from human genetics. Nat Rev Genet 7(1):45–54 53. Ochi T, Sibanda BL, Wu Q, Chirgadze DY, Bolanos-Garcia VM, Blundell TL (2010) Structural biology of DNA repair: spatial organisation of the multicomponent complexes of nonhomologous End joining, J Nucleic Acids 2010:1–19 54. Pascal JM, O’Brien PJ, Tomkinson AE, Ellenberger T (2004) Human DNA ligase I completely encircles and partially unwinds nicked DNA. Nature 432(7016):473–478 55.

Menetret JF, Schaletzky J, Clemons WM Jr, Osborne AR, Skanland SS, Denison C, Gygi SP, Kirkpatrick DS, Park E, Ludtke SJ et al (2007) Ribosome binding of a single copy of the SecY complex: implications for protein translocation. Mol Cell 28:1083–1092 33. Merz F, Boehringer D, Schaffitzel C, Preissler S, Hoffmann A, Maier T, Rutkowska A, Lozza J, Ban N, Bukau B et al (2008) Molecular mechanism and structure of trigger factor bound to the translating ribosome. EMBO J 27:1622–1632 34. Merz F, Hoffmann A, Rutkowska A, Zachmann-Brand B, Bukau B, Deuerling E (2006) The C-terminal domain of Escherichia coli trigger factor represents the central module of its chaperone activity.

It is not clear whether the XLF-dimer interactions with XRCC4-dimer are maintained when the ligase is recruited. Protein interaction assays have confirmed the XRCC4-independent XLF recruitment to DSBs ends through interaction with Ku only in the presence of DNA, so XLF may act independently of XRCC4. 1 Discussion Multiprotein Systems and New Approaches to Structure Analysis Our observations of NHEJ repair are typical of many cell regulation systems. Large numbers of protein, nucleic acid and other components tend to assemble and disassemble, requiring the ability to describe a series of transient complexes in both space and time.

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Macromolecular Crystallography: Deciphering the Structure, Function and Dynamics of Biological Molecules by Qian Wu, Lynn Sibanda, Takashi Ochi (auth.), Maria Armenia Carrondo, Paola Spadon (eds.)

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