6 Publikationen

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  • [6]
    2022 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2961733 OA
    Geerds, C., Bleymüller, W. M., Meyer, T., Widmann, C., & Niemann, H. (2022). A recurring packing contact in crystals of InlB pinpoints functional binding sites in the internalin domain and the B repeat. Acta Crystallographica Section D : Structural Biology , 78( 3), 310-320. https://doi.org/10.1107/S2059798322000432
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  • [5]
    2021 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2956908 OA
    Geerds, C., Haas, A., & Niemann, H. (2021). Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB. Acta crystallographica. Section F: Structural biology communications, 77(Pt 8), 246-253. https://doi.org/10.1107/S2053230X2100738X
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  • [4]
    2020 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2945148 OA
    Meyer, T., Zumbrägel, N., Geerds, C., Gröger, H., & Niemann, H. (2020). Structural Characterization of an S-enantioselective Imine Reductase from Mycobacterium Smegmatis. Biomolecules, 10(8), 1130. doi:10.3390/biom10081130
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  • [3]
    2018 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2920494
    Buß, M., Geerds, C., Patschkowski, T., Niehaus, K., & Niemann, H. (2018). Perfect merohedral twinning combined with noncrystallographic symmetry potentially causes the failure of molecular replacement with low-homology search models for the flavin-dependent halogenase HalX from Xanthomonas campestris. Acta Crystallographica Section F Structural Biology Communications, 74(6), 345-350. doi:10.1107/s2053230x18006933
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  • [2]
    2016 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2907323
    Bleymüller, W., Lämmermann, N., Ebbes, M., Maynard, D., Geerds, C., & Niemann, H. (2016). MET-activating Residues in the B-repeat of theListeria monocytogenesInvasion Protein InlB. Journal of Biological Chemistry, 291(49), 25567-25577. doi:10.1074/jbc.m116.746685
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  • [1]
    2014 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2685751
    Geerds, C., Wohlmann, J., Haas, A., & Niemann, H. (2014). Structure of Rhodococcus equi virulence-associated protein B (VapB) reveals an eight-stranded antiparallel β-barrel consisting of two Greek-key motifs. Acta crystallographica. Section F, Structural biology communications, 70(Pt 7), 866-871. doi:10.1107/S2053230X14009911
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