Research output per year
Research output per year
Bergmann Justin, Max Davidson, Esko Oksanen, Ulf Ryde, Dylan Jayatilaka
Research output: Contribution to journal › Article › peer-review
The first ab initio aspherical structure refinement against experimental X-ray structure factors for polypeptides and proteins using a fragmentation approach to break up the protein into residues and solvent, thereby speeding up quantum-crystallographic Hirshfeld atom refinement (HAR) calculations, is described. It it found that the geometric and atomic displacement parameters from the new fragHAR method are essentially unchanged from a HAR on the complete unfragmented system when tested on dipeptides, tripeptides and hexapeptides. The largest changes are for the parameters describing H atoms involved in hydrogen-bond interactions, but it is shown that these discrepancies can be removed by including the interacting fragments as a single larger fragment in the fragmentation scheme. Significant speed-ups are observed for the larger systems. Using this approach, it is possible to perform a highly parallelized HAR in reasonable times for large systems. The method has been implemented in the TONTO software.
Original language | English |
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Pages (from-to) | 158-165 |
Number of pages | 8 |
Journal | IUCrJ |
Volume | 7 |
Issue number | 2 |
DOIs | |
Publication status | Published - 2020 Mar |
Research output: Thesis › Doctoral Thesis (compilation)