Christian Betzel
University of Hamburg
349 Papers
2.8K Citations
Christian Betzel is an academic researcher from University of Hamburg. The author has contributed to research in topics: Protein crystallization & Chemistry. The author has an hindex of 44, co-authored 330 publications. Previous affiliations of Christian Betzel include Eppendorf (Germany) & University of Tübingen.
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Papers
Fluorescence properties of native and photooxidised proteinase K: the X-ray model in the region of the two tryptophans.
TL;DR: The fluorescence properties of proteinase K are described and related to the X-ray model refined at 1.48 A resolution and the data show homogeneity of the indole fluorescence arising from fluorophores in similar environments.
Differences in the specificities of the highly alkalophilic proteinases Savinase and Esperase imposed by changes in the rigidity and geometry of the substrate binding sites.
TL;DR: The lower affinity and catalytic efficiency as well as more narrow proteolytic specificity of Savinase in comparison to those of Esperase are explained with the extra rigidity and unfavorable changes in geometry of the substrate binding site of the first enzyme.
Mistletoe lectin I in complex with galactose and lactose reveals distinct sugar-binding properties
Ruth Mikeska,Roland Wacker,Raghuvir K. Arni,Tej P. Singh,Al'bert M. Mikhailov,A.G. Gabdoulkhakov,Wolfgang Voelter,Christian Betzel +7 more
TL;DR: A potential third low-affinity galactose-binding site in subunit beta1 was identified in the present ML-I structures, in which a glycerol molecule from the cryoprotectant buffer has bound, mimicking the sugar compound.
Analysis of self-assembly of S-layer protein slp-B53 from Lysinibacillus sphaericus
Jun Liu,Sven Falke,Bjoern Drobot,Dominik Oberthuer,Alexey Kikhney,Tobias Guenther,Karim Fahmy,Dmitri I. Svergun,Christian Betzel,Johannes Raff +9 more
TL;DR: The results obtained highlight potential applications of S-layers in the fields of micromaterials and nanobiotechnology by providing engineered or individual symmetric thin protein layers, e.g., for protective, antimicrobial, or otherwise functionalized surfaces.
Crystal structure of a novel myotoxic Arg49 phospholipase A2 homolog (zhaoermiatoxin) from Zhaoermia mangshanensis snake venom: insights into Arg49 coordination and the role of Lys122 in the polarization of the C-terminus.
TL;DR: The first crystal structure of zhaoermiatoxin, an Arg49-PLA2, from Zhaoermia mangshanensis venom is determined at 2.05 angstroms resolution, which represents a novel member of phospholipase A2 family.