Sine Larsen
University of Copenhagen
287 Papers
2.1K Citations
Sine Larsen is an academic researcher from University of Copenhagen. The author has contributed to research in topics: Crystal structure & Chemistry. The author has an hindex of 38, co-authored 287 publications. Previous affiliations of Sine Larsen include European Synchrotron Radiation Facility & European Bioinformatics Institute.
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Papers
The binding of zinc ions to Emericella nidulans endo-β-1,4-galactanase is essential for crystal formation.
TL;DR: The crystal structure showed a high similarity between EnGAL and other endo-β-1,4-galactanases belonging to GH53 and revealed 15 zinc ions bound to the protein, one of which is located in the active site, where it is coordinated by residues Glu136 and Glu246 which comprise the catalytic machinery.
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Structures with identical packing; racemic and partially optically pure 3-(2'-chloro-2'-phenylethyl)-2-thiazolidiniminium p-toluenesulfonate and a comparison of the packing in corresponding racemic and optically active compounds
TL;DR: In this paper, the crystal structures of 3-chloro-2'-phenylethyl)-2-thiazolidiniminium p-toluenesulfonate (C 11 H 14 ClN 2 S +.C 7 H 7 O 3 S - ) from low-temperature (122 K) X-ray diffraction data were determined for racemic and two optically active samples.
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The Optical Resolution of 3-(2'-Hydroxy-2'-phenylethyl)-2-thiazolidinimine and the Crystal Structure of the (2R,3R)-O,O'-Dibenzoyl Hydrogen Tartrate Salt of the (S)-(+)-Enantiomer.
The structure of a mutant enzyme of Coprinus cinereus peroxidase provides an understanding of its increased thermostability.
Karen Houborg,Pernille Harris,Jens-Christian N. Poulsen,Palle Schneider,Allan Svendsen,Sine Larsen +5 more
TL;DR: The mutant enzyme (TS-rCiP) is a mutant enzyme which is more stable than the native enzyme at higher temperature, pH and hydrogen peroxide concentrations and is therefore more suitable for industrial applications.
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