By Qian Wu, Lynn Sibanda, Takashi Ochi (auth.), Maria Armenia Carrondo, Paola Spadon (eds.)
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 new release on complex tools and methods for interpreting structural and dynamic elements of organic macromolecules. The papers evaluation the options used to check 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 during the publication is the dependence of contemporary structural technology on a number of experimental and computational strategies, and it's the improvement of those recommendations and their integration that may take us ahead within the future.
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Additional resources for Macromolecular Crystallography: Deciphering the Structure, Function and Dynamics of Biological Molecules
Spagnolo L, Rivera-Calzada A, Pearl LH, Llorca O (2006) Three-dimensional structure of the human dna-pkcs/ku70/ku80 complex assembled on DNA and its implications for DNA dsb repair. Mol Cell 22(4):511–519 78. Suchanek M, Radzikowska A, Thiele C (2005) Photo-leucine and photo-methionine allow identification of protein-protein interactions in living cells. Nat Methods 2(4):261–267. 1038/nmeth752 79. Svergun DI, Koch MHJ (2003) Small-angle scattering studies of biological macromolecules in solution.
GraFix, ultracentrifugation in solutions with glycerol and fixation gradients is a recently developed method to provide homogeneous samples, and can improve the quality of EM images . Model building into EM maps can be achieved with and without crystallographic structures [46, 68]. As a guide of the modeling, hexahistidine tags and DNA labeled with gold clusters (Nanoprobes) allow the location of the tags and DNA in complexes. In reverse, EM maps have been successfully used for phasing X-ray diffraction data by molecular replacement [51, 88].
The region of the XRCC4 C-terminal domain after residue 213 is not included in current solved XRCC4 crystal structures due to its predicted flexible structure. XRCC4 can exist as a salt-dependent equilibrium of dimers and tetramers in solution . The dynamic of XRCC4 oligomers formation can be also shifted to dimmers through strong binding of LigIV to XRCC4 C-terminal helices . The binding region between XRCC4 and LigIV overlaps with the XRCC4 tetramerisation region, which may explain why LigIV functions as a strong competitor to shift the equilibrium towards the XRCC4 dimer in solution  (Fig.