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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
<em>IceBear</em>: an intuitive and versatile web application for research-data tracking from crystallization experiment to PDB deposition
Daniel, E., Maksimainen, M. M., Smith, N., Ratas, V., Biterova, E., Murthy, S. N., … Wierenga, R. K. (2021). IceBear: an intuitive and versatile web application for research-data tracking from crystallization experiment to PDB deposition. Acta Crystallographica Section D: Structural Biology, 77, 151-163. https://doi.org/10.1107/S2059798320015223
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
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
Exploring the complex map of insulin polymorphism: a novel crystalline form in the presence of <em>m</em>-cresol
Karavassili, F., Valmas, A., Dimarogona, M., Giannopoulou, A. E., Fili, S., Norrman, M., … Margiolaki, I. (2020). Exploring the complex map of insulin polymorphism: a novel crystalline form in the presence of m-cresol. Acta Crystallographica Section D: Structural Biology, 76, 366-374. https://doi.org/10.1107/S2059798320002545
The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography
Mehr, A., Henneberg, F., Chari, A., Görlich, D., & Huyton, T. (2020). The copper(II)-binding tripeptide GHK, a valuable crystallization and phasing tag for macromolecular crystallography. Acta Crystallographica Section D: Structural Biology, 76(12), 1222-1232. https://doi.org/10.1107/S2059798320013741
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
Design guidelines for an electron diffractometer for structural chemistry and structural biology
Heidler, J., Pantelic, R., Wennmacher, J. T. C., Zaubitzer, C., Fecteau-Lefebvre, A., Goldie, K. N., … Gruene, T. (2019). Design guidelines for an electron diffractometer for structural chemistry and structural biology. Acta Crystallographica Section D: Structural Biology, 75(5), 458-466. https://doi.org/10.1107/S2059798319003942
Crystal structure of the leucine-rich repeat ectodomain of the plant immune receptor kinase SOBIR1
Hohmann, U., & Hothorn, M. (2019). Crystal structure of the leucine-rich repeat ectodomain of the plant immune receptor kinase SOBIR1. Acta Crystallographica Section D: Structural Biology, 75(5), 488-497. https://doi.org/10.1107/S2059798319005291
Strategies for sample delivery for femtosecond crystallography
Martiel, I., Müller-Werkmeister, H. M., & Cohen, A. E. (2019). Strategies for sample delivery for femtosecond crystallography. Acta Crystallographica Section D: Structural Biology, 75(2), 160-177. https://doi.org/10.1107/S2059798318017953
Radiation damage in protein crystallography at X-ray free-electron lasers
Nass, K. (2019). Radiation damage in protein crystallography at X-ray free-electron lasers. Acta Crystallographica Section D: Structural Biology, 75(2), 211-218. https://doi.org/10.1107/S2059798319000317
Crystal structure of the pseudoenzyme PDX1.2 in complex with its cognate enzyme PDX1.3: a total eclipse
Robinson, G. C., Kaufmann, M., Roux, C., Martinez-Font, J., Hothorn, M., Thore, S., & Fitzpatrick, T. B. (2019). Crystal structure of the pseudoenzyme PDX1.2 in complex with its cognate enzyme PDX1.3: a total eclipse. Acta Crystallographica Section D: Structural Biology, 75(4), 400-415. https://doi.org/10.1107/S2059798319002912
Electron diffraction data processing with <em>DIALS</em>
Clabbers, M. T. B., Gruene, T., Parkhurst, J. M., Abrahams, J. P., & Waterman, D. G. (2018). Electron diffraction data processing with DIALS. Acta Crystallographica Section D: Structural Biology, 74(6). https://doi.org/10.1107/S2059798318007726
Structural rearrangements occurring upon cofactor binding in the <i>Mycobacterium smegmatis β</i>-ketoacyl-acyl carrier protein reductase MabA
Küssau, T., Flipo, M., Van Wyk, N., Viljoen, A., Olieric, V., Kremer, L., & Blaise, M. (2018). Structural rearrangements occurring upon cofactor binding in the Mycobacterium smegmatis β-ketoacyl-acyl carrier protein reductase MabA. Acta Crystallographica Section D: Structural Biology, D74(Part 5), 383-393. https://doi.org/10.1107/S2059798318002917
Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction
Moussu, S., Augustin, S., Roman, A. O., Broyart, C., & Santiago, J. (2018). Crystal structures of two tandem malectin-like receptor kinases involved in plant reproduction. Acta Crystallographica Section D: Structural Biology, 74(7), 671-680. https://doi.org/10.1107/S205979831800774X
Domain swap in the C-terminal ubiquitin-like domain of human doublecortin
Rufer, A. C., Kusznir, E., Burger, D., Stihle, M., Ruf, A., & Rudolph, M. G. (2018). Domain swap in the C-terminal ubiquitin-like domain of human doublecortin. Acta Crystallographica Section D: Structural Biology, 74(5), 450-462. https://doi.org/10.1107/S2059798318004813
Protein structure determination by electron diffraction using a single three-dimensional nanocrystal
Clabbers, M. T. B., van Genderen, E., Wan, W., Wiegers, E. L., Gruene, T., & Abrahams, J. P. (2017). Protein structure determination by electron diffraction using a single three-dimensional nanocrystal. Acta Crystallographica Section D: Structural Biology, 73(9), 738-748. https://doi.org/10.1107/S2059798317010348
A standardized technique for high-pressure cooling of protein crystals
Quirnheim Pais, D., Rathmann, B., Koepke, J., Tomova, C., Wurzinger, P., & Thielmann, Y. (2017). A standardized technique for high-pressure cooling of protein crystals. Acta Crystallographica Section D: Structural Biology, 73(12), 997-1006. https://doi.org/10.1107/S2059798317016357
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
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
 

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