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Structure of BamA, an essential factor in outer membrane protein biogenesis
Albrecht, R., Schütz, M., Oberhettinger, P., Faulstich, M., Bermejo, I., Rudel, T., … Zeth, K. (2014). Structure of BamA, an essential factor in outer membrane protein biogenesis. Acta Crystallographica Section D: Structural Biology, 70(6), 1779-1789. https://doi.org/10.1107/S1399004714007482
Combination of X-ray crystallography, SAXS and DEER to obtain the structure of the FnIII-3,4 domains of integrin <em>α</em>6<em>β</em>4
Alonso-García, N., García-Rubio, I., Manso, J. A., Buey, R. M., Urien, H., Sonnenberg, A., … de Pereda, J. M. (2015). Combination of X-ray crystallography, SAXS and DEER to obtain the structure of the FnIII-3,4 domains of integrin α6β4. Acta Crystallographica Section D: Structural Biology, 71, 969-985. https://doi.org/10.1107/S1399004715002485
Identification of the first small-molecule ligand of the neuronal receptor sortilin and structure determination of the receptor-ligand complex
Andersen, J. L., Schrøder, T. J., Christensen, S., Strandbygård, D., Pallesen, L. T., García-Alai, M. M., … Thirup, S. (2014). Identification of the first small-molecule ligand of the neuronal receptor sortilin and structure determination of the receptor-ligand complex. Acta Crystallographica Section D: Structural Biology, 70(2), 451-460. https://doi.org/10.1107/S1399004713030149
Making a difference in multi-data-set crystallography: simple and deterministic data-scaling/selection methods
Assmann, G. M., Wang, M., & Diederichs, K. (2020). Making a difference in multi-data-set crystallography: simple and deterministic data-scaling/selection methods. Acta Crystallographica Section D: Structural Biology, 76, 636-652. https://doi.org/10.1107/S2059798320006348
Atomic resolution structure of a lysine-specific endoproteinase from<em> Lysobacter enzymogenes </em>suggests a hydroxyl group bound to the oxyanion hole
Asztalos, P., Müller, A., Hölke, W., Sobek, H., & Rudolph, M. G. (2014). Atomic resolution structure of a lysine-specific endoproteinase from Lysobacter enzymogenes suggests a hydroxyl group bound to the oxyanion hole. Acta Crystallographica Section D: Structural Biology, 70(7), 1832-1843. https://doi.org/10.1107/S1399004714008463
Mapping the conformational space accessible to BACE2 using surface mutants and cocrystals with Fab fragments, Fynomers and Xaperones
Banner, D. W., Gsell, B., Benz, J., Bertschinger, J., Burger, D., Brack, S., … Ruf, A. (2013). Mapping the conformational space accessible to BACE2 using surface mutants and cocrystals with Fab fragments, Fynomers and Xaperones. Acta Crystallographica Section D: Structural Biology, 69(6), 1124-1137. https://doi.org/10.1107/S0907444913006574
Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ
Barends, T. R. M., Brosi, R. W. W., Steinmetz, A., Scherer, A., Hartmann, E., Eschenbach, J., … Reinstein, J. (2013). Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ. Acta Crystallographica Section D: Structural Biology, 69(8), 1540-1552. https://doi.org/10.1107/S0907444913010640
Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source
Basu, S., Finke, A., Vera, L., Wang, M., & Olieric, V. (2019). Making routine native SAD a reality: lessons from beamline X06DA at the Swiss Light Source. Acta Crystallographica Section D: Structural Biology, 75(3), 262-271. https://doi.org/10.1107/S2059798319003103
Macromolecular X-ray crystallography: soon to be a road less travelled?
Beale, J. H. (2020). Macromolecular X-ray crystallography: soon to be a road less travelled? Acta Crystallographica Section D: Structural Biology, 76(5), 400-405. https://doi.org/10.1107/S2059798320004660
The magic triangle goes MAD: experimental phasing with a bromine derivative
Beck, T., Gruene, T., & Sheldrick, G. M. (2010). The magic triangle goes MAD: experimental phasing with a bromine derivative. Acta Crystallographica Section D: Structural Biology, 66(4), 374-380. https://doi.org/10.1107/S0907444909051609
Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals
Blum, T. B., Housset, D., Clabbers, M. T. B., van Genderen, E., Bacia-Verloop, M., Zander, U., … Abrahams, J. P. (2021). Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals. Acta Crystallographica Section D: Structural Biology, 77, 75-85. https://doi.org/10.1107/S2059798320014540
Room-temperature serial crystallography at synchrotron X-ray sources using slowly flowing free-standing high-viscosity microstreams
Botha, S., Nass, K., Barends, T., Kabsch, W., Latz, B., Dworkowski, F., … Doak, R. B. (2015). Room-temperature serial crystallography at synchrotron X-ray sources using slowly flowing free-standing high-viscosity microstreams. Acta Crystallographica Section D: Structural Biology, 71, 387-397. https://doi.org/10.1107/S1399004714026327
Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90
Bracher, A., Kozany, C., Thost, A. K., & Hausch, F. (2011). Structural characterization of the PPIase domain of FKBP51, a cochaperone of human Hsp90. Acta Crystallographica Section D: Structural Biology, 67(6), 549-559. https://doi.org/10.1107/S0907444911013862
Breaking the indexing ambiguity in serial crystallography
Brehm, W., & Diederichs, K. (2014). Breaking the indexing ambiguity in serial crystallography. Acta Crystallographica Section D: Structural Biology, 70(1), 101-109. https://doi.org/10.1107/S1399004713025431
Structure-function studies of the RNA polymerase II elongation complex
Brueckner, F., Armache, K. J., Cheung, A., Damsma, G. E., Kettenberger, H., Lehmann, E., … Cramer, P. (2009). Structure-function studies of the RNA polymerase II elongation complex. Acta Crystallographica Section D: Structural Biology, 65(2), 112-120. https://doi.org/10.1107/S0907444908039875
Tackling the crystallographic structure determination of the COP9 signalosome
Bunker, R. D. (2016). Tackling the crystallographic structure determination of the COP9 signalosome. Acta Crystallographica Section D: Structural Biology, 72(3), 326-335. https://doi.org/10.1107/S2059798316001169
Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre
Båth, P., Banacore, A., Börjesson, P., Bosman, R., Wickstrand, C., Safari, C., … Neutze, R. (2022). Lipidic cubic phase serial femtosecond crystallography structure of a photosynthetic reaction centre. Acta Crystallographica Section D: Structural Biology, 78(6), 698-708. https://doi.org/10.1107/S2059798322004144
EIGER detector: application in macromolecular crystallography
Casanas, A., Warshamanage, R., Finke, A. D., Panepucci, E., Olieric, V., Nöll, A., … Wang, M. (2016). EIGER detector: application in macromolecular crystallography. Acta Crystallographica Section D: Structural Biology, 72(9), 1036-1048. https://doi.org/10.1107/S2059798316012304
Discovery of a novel allosteric inhibitor-binding site in ERK5: comparison with the canonical kinase hinge ATP-binding site
Chen, H., Tucker, J., Wang, X., Gavine, P. R., Phillips, C., Augustin, M. A., … Ogg, D. (2016). Discovery of a novel allosteric inhibitor-binding site in ERK5: comparison with the canonical kinase hinge ATP-binding site. Acta Crystallographica Section D: Structural Biology, 72(5), 682-693. https://doi.org/10.1107/S2059798316004502
Structural evidence for asymmetric ligand binding to transthyretin
Cianci, M., & Zanotti, G. (2015). Structural evidence for asymmetric ligand binding to transthyretin. Acta Crystallographica Section D: Structural Biology, 71, 1582-1592. https://doi.org/10.1107/S1399004715010585
 

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