Logan DT

Nucleotide binding to the ATP-cone in anaerobic ribonucleotide reductases allosterically regulates activity by modulating substrate binding

Bimai O, Banerjee I, Rozman Grinberg I, ..., Sjöberg BM, Logan DT

Elife 12 (-) - [2024-07-05; online 2024-07-05]

Cryo-EM [Service] Structural Proteomics [Service]

A nucleotide-sensing oligomerization mechanism that controls NrdR-dependent transcription of ribonucleotide reductases.

Rozman Grinberg I, Martínez-Carranza M, Bimai O, ..., Sjöberg BM, Stenmark P

Nat Commun 13 (1) 2700 [2022-05-16; online 2022-05-16]

Cryo-EM [Service]

Solution Structure of the dATP-Inactivated Class I Ribonucleotide Reductase From Leeuwenhoekiella blandensis by SAXS and Cryo-Electron Microscopy.

Hasan M, Banerjee I, Rozman Grinberg I, Sjöberg BM, Logan DT

Front Mol Biosci 8 (-) 713608 [2021-07-26; online 2021-07-26]

Cryo-EM [Service]

Entropy-Entropy Compensation between the Protein, Ligand, and Solvent Degrees of Freedom Fine-Tunes Affinity in Ligand Binding to Galectin-3C.

Wallerstein J, Ekberg V, Ignjatović MM, ..., Ryde U, Akke M

JACS Au 1 (4) 484-500 [2021-04-26; online 2021-04-01]

Swedish NMR Centre (SNC) [Collaborative]

Interplay between Conformational Entropy and Solvation Entropy in Protein-Ligand Binding.

Verteramo ML, Stenström O, Ignjatović MM, ..., Ryde U, Akke M

J. Am. Chem. Soc. 141 (5) 2012-2026 [2019-02-06; online 2019-01-23]

Swedish NMR Centre (SNC) [Service]