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• [6]
  

  2022 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2961733

  Geerds, Christina, Bleymüller, Willem M, Meyer, Timo, Widmann, Christiane, and Niemann, Hartmut. “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 (2022): 310-320.

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• [5]
  

  2021 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2956908

  Geerds, Christina, Haas, Albert, and Niemann, Hartmut. “Conformational changes of loops highlight a potential binding site in Rhodococcus equi VapB”. Acta crystallographica. Section F: Structural biology communications 77.Pt 8 (2021): 246-253.

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• [4]
  

  2020 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2945148

  Meyer, Timo, Zumbrägel, Nadine, Geerds, Christina, Gröger, Harald, and Niemann, Hartmut. “Structural Characterization of an S-enantioselective Imine Reductase from Mycobacterium Smegmatis”. Biomolecules 10.8 (2020): 1130.

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• [3]
  

  2018 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2920494

  Buß, Maren, Geerds, Christina, Patschkowski, Thomas, Niehaus, Karsten, and Niemann, Hartmut. “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 (2018): 345-350.

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• [2]
  

  2016 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2907323

  Bleymüller, Willem, Lämmermann, Nina, Ebbes, Maria, Maynard, Daniel, Geerds, Christina, and Niemann, Hartmut. “MET-activating Residues in the B-repeat of theListeria monocytogenesInvasion Protein InlB”. Journal of Biological Chemistry 291.49 (2016): 25567-25577.

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• [1]
  

  2014 | Zeitschriftenaufsatz | Veröffentlicht | PUB-ID: 2685751

  Geerds, Christina, Wohlmann, Jens, Haas, Albert, and Niemann, Hartmut. “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 (2014): 866-871.

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