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Body temperature protein X-ray crystallography at 37 °C: a rhenium protein complex seeking a physiological condition structure
The retention of the covalent binding of an organometalllic rhenium complex as a model for a technetium-99m imaging agent, to a protein at physiological body temperature 37 °C is described. Detailed structure comparisons are made to the related 100 K crystal structure. The generality of the need for...
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Published in: | Chemical communications (Cambridge, England) England), 2024-11, Vol.6 (95), p.143-1433 |
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Main Authors: | , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites |
Online Access: | Get full text |
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Summary: | The retention of the covalent binding of an organometalllic rhenium complex as a model for a technetium-99m imaging agent, to a protein at physiological body temperature 37 °C is described. Detailed structure comparisons are made to the related 100 K crystal structure. The generality of the need for this sort of analytical procedure for guiding ligand lead compound discovery is emphasised.
The retention of the covalent binding of an organometalllic rhenium complex to a protein at physiological body temperature (37 °C) is described and compared to the related 100 K crystal structure. |
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ISSN: | 1359-7345 1364-548X 1364-548X |
DOI: | 10.1039/d4cc04245j |