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Bernhard Lohkamp
Researcher at Karolinska Institutet
Publications - 28
Citations - 22962
Bernhard Lohkamp is an academic researcher from Karolinska Institutet. The author has contributed to research in topics: Active site & Thymine. The author has an hindex of 15, co-authored 26 publications receiving 18345 citations. Previous affiliations of Bernhard Lohkamp include Nanyang Technological University & University of Glasgow.
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Journal ArticleDOI
Features and development of Coot.
TL;DR: Coot is a molecular-graphics program designed to assist in the building of protein and other macromolecular models and the current state of development and available features are presented.
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Current Developments in Coot for Macromolecular Model Building of Electron Cryo‐microscopy and Crystallographic Data
TL;DR: The current state‐of‐the‐art in Coot usage is presented, including morphing, Geman‐McClure restraints, full‐chain refinement, and Fourier‐model based residue‐type‐specific Ramachandran restraints.
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The Crystal Structures of Dihydropyrimidinases Reaffirm the Close Relationship between Cyclic Amidohydrolases and Explain Their Substrate Specificity
TL;DR: The extension of one of the sheets of the β-sandwich domain across a subunit-subunit interface in yeast dihydropyrimidinase underlines its closer evolutionary relationship to hydantoinases, whereas the slime mold enzyme shows higher similarity to the noncatalytic collapsin-response mediator proteins involved in neuron development.
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The structure of Escherichia coli ATP-phosphoribosyltransferase: identification of substrate binding sites and mode of AMP inhibition.
TL;DR: Comparison with the recently solved Mycobacterium tuberculosis ATP-PRT structures indicates that histidine is solely responsible for the large conformational changes observed between the hexameric forms of the enzyme.
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Ab initio solution of macromolecular crystal structures without direct methods.
Airlie J. McCoy,Robert D. Oeffner,A.G. Wrobel,Juha R.M. Ojala,Karl Tryggvason,Karl Tryggvason,Bernhard Lohkamp,Randy J. Read +7 more
TL;DR: It is now possible to make an accurate prediction of whether or not a molecular replacement solution of a macromolecular crystal structure will succeed, given the quality of the model, its size, and the resolution of the diffraction data, according to the signal-to-noise ratio.