2025

Contaldo U, Guigliarelli B, Perard J, Pichon T, Le Goff A, Cavazza C. Insights into the Role of the D-Cluster in [NiFe]-CODH from Rhodospirillum Rubrum. Chemistry, e202403648 (2025) online ahead of print. https://doi.org/10.1002/chem.202403648

Coquille S, Pereira CS, Roche J, Santoni G, Engilberge S, Brochier-Armanet C, Girard E, Sterpone F, Madern D. Allostery and Evolution: A Molecular Journey Through the Structural and Dynamical Landscape of an Enzyme Super Family. Mol. Biol. Evol. 42, msae265 (2025) https://doi.org/10.1093/molbev/msae265

Franke P, Freiberger S, Zhang L, Einsle O. Conformational protection of molybdenum nitrogenase by Shethna protein II (2025) Nature 637, 998-1004 (2025) https://doi.org/10.1038/s41586-024-08355-3

Genz F, Friedrich F, Lönarz C, Einsle O, Jung M, Müller M, Fessner ND. Identification and Characterization of Pyrimidine Nucleoside 2′-Hydroxylase. ACS Catalysis 15, 3611-3618 (2025) https://doi.org/10.1021/acscatal.4c07764

 

2024

Bolton R, Machelett MM, Stubbs J, Axford D, Caramello N, Catapano L, Malý M, Rodrigues MJ, Cordery C, Tizzard GJ, MacMillan F, Engilberge S, von Stetten D, Tosha T, Sugimoto H, Worrall JAR, Webb JS, Zubkov M, Coles S, Mathieu E, Steiner RA, Murshudov G, Schrader TE, Orville AM, Royant A, Evans G, Hough MA, Owen RL, Tews I. A redox switch allows binding of Fe(II) and Fe(III) ions in the cyanobacterial iron-binding protein FutA from Prochlorococcus. Proc. Natl Acad. Sci. USA 121, e2308478121 (2024) https://doi.org/10.1073/pnas.2308478121

Catalini S, Bagni F, Cicchi S, Di Donato M, Iagatti A, Lapini A, Foggi P, Petrillo C, Di Michele A, Paolantoni M, Schirò G, Comez L, Paciaroni A. Multiple length-scale control of Boc-protected diphenylalanine aggregates through solvent composition. Mater. Adv. 5, 3802-3811 (2024) https://doi.org/10.1039/D4MA00018H

Huang CY, Aumonier S, Olieric V, Wang M. Cryo2RT: a high-throughput method for room-temperature macromolecular crystallography from cryo-cooled crystals. Acta Crystallogr. D Struct. Biol. 80, 620-628. https://doi.org/10.1107/S2059798324006697

Lenka DR, Dahe SV, Antico O, Sahoo P, Prescott AR, Muqit MMK, Kumar A. Additional feedforward mechanism of Parkin activation via binding of phospho-UBL and RING0 in trans. Elife 13, RP96699 (2024) https://doi.org/10.7554/eLife.96699

Lublin V, Kauffmann B, Engilberge S, Durola F, Gounel S, Bichon S, Jean C, Mano N, Giraud MF, Chavas LMGH, Thureau A, Thompson A, Stines-Chaumeil C. Does Acinetobacter calcoaceticus glucose dehydrogenase produce self-damaging H2O2? Biosci. Rep. 44, BSR20240102 (2024) https://doi.org/10.1042/BSR20240102

Mohanlal S, Saha D, Pandey S, Acharya R, Sharma NK. Synthesis of R-GABA Derivatives via Pd(II) Catalyzed Enantioselective C(sp3)-H Arylation and Virtual Validation with GABAB1 Receptor for Potential leads. Chem. Asian J. 19, e202400064 (2024) https://doi.org/10.1002/asia.202400064

Montserrat-Canals M, Bjerregaard-Andersen K, Sørensen HV, Kommedal E, Cordara G, Vaaje-Kolstad G, Krengel U. Calcium-binding site in AA10 LPMO from Vibrio cholerae suggests modulating effects during environmental survival and infection. QRB Discov. 5, e12 (2024) https://doi.org/10.1017/qrd.2024.14

Munzone A, Pujol M, Tamhankar A, Joseph C, Mazurenko I, Réglier M, Jannuzzi SAV, Royant A, Sicoli G, DeBeer S, Orio M, Simaan AJ, Decroos C. Integrated Experimental and Theoretical Investigation of Copper Active Site Properties of a Lytic Polysaccharide Monooxygenase from Serratia marcescens. Inorg. Chem. 63, 11063-11078 (2024) http://doi.org10.1021/acs.inorgchem.4c00602.

Muradova M, Poirier N, Moreno J, Proskura A, Lirussi F, Heydel JM, Baranenko D, Nadtochii L, Neiers F, Schwartz M. Crystallization and Preliminary X-ray Diffraction Study of a Putative β-glycosidase from the Oral Bacteria Prevotella sp. Crystallogr. Rep. 69, 507-512 (2024)

Pachl P, Coudray L, Vincent R, Nilles L, Scheer H, Ritzenthaler C, Fejfarová A, Řezáčová P, Engilberge S, Sauter C. Protein crystallization and structure determination at room temperature in the CrystalChip. FEBS Open Bio (2024) online ahead of print. https://doi.org/10.1002/2211-5463.13932

Poirier N, Ménétrier F, Moreno J, Boichot V, Heydel JM, Didierjean C, Canivenc-Lavier MC, Canon F, Neiers F, Schwartz M. Rattus norvegicus Glutathione Transferase Omega 1 Localization in Oral Tissues and Interactions with Food Phytochemicals. J. Agric. Food Chem. 72, 5887-5897 (2024) https://doi.org/10.1021/acs.jafc.4c00483

Pomyalov S, Minetti CA, Remeta DP, Bonala R, Johnson F, Zaitseva I, Iden C, Golebiewska U, Breslauer KJ, Shoham G, Sidorenko VS, Grollman AP. Structural and mechanistic insights into the transport of aristolochic acids and their active metabolites by human serum albumin. J. Biol. Chem. 300, 107358 (2024) http://doi.org/10.1016/j.jbc.2024.107358

Reinke PYA, Heiringhoff RS, Reindl T, Baker K, Taft MH, Meents A, Mulvihill DP, Davies OR, Fedorov R, Zahn M, Manstein DJ. Crystal structures of cables formed by the acetylated and unacetylated forms of the Schizosaccharomyces pombe tropomyosin ortholog TpmCdc8. J. Biol. Chem. 300, 107925 (2024) https://doi.org/10.1016/j.jbc.2024.107925

Roger M, Leone P, Blackburn NJ, Horrell S, Chicano TM, Biaso F, Giudici-Orticoni MT, Abriata LA, Hura GL, Hough MA, Sciara G, Ilbert M. Beyond the coupled distortion model: structural analysis of the single domain cupredoxin AcoP, a green mononuclear copper centre with original features. Dalton Trans. 53, 1794-1808 (2024) https://doi.org/10.1039/d3dt03372d

 

2023

Bertrand Q, Coquille S, Iorio A, Sterpone F, Madern D (2023) Biochemical, structural and dynamical characterizations of the lactate dehydrogenase from Selenomonas ruminantium provide information about an intermediate evolutionary step prior to complete allosteric regulation acquisition in the super family of lactate and malate dehydrogenases. J. Struct. Biol. 215:108039. https://doi.org/10.1016/j.jsb.2023.108039

Garman EF, Weik M (2023) Radiation damage to biological macromolecules. Curr. Opin. Struct. Biol. 82:102662 https://doi.org/10.1016/j.sbi.2023.102662

Goudiaby I, Malliavin TE, Mocchetti E, Mathiot S, Acherar S, Frochot C, Barberi-Heyob M, Guillot B, Favier F, Didierjean C, Jelsch C (2023) New Crystal Form of Human Neuropilin-1 b1 Fragment with Six Electrostatic Mutations Complexed with KDKPPR Peptide Ligand. Molecules 28:5603. https://doi.org/10.3390/molecules28145603

Omeiri J, Martin L, Usclat A, Cherrier MV, Nicolet Y (2023) Maturation of the [FeFe]-Hydrogenase: Direct Transfer of the (κ3-cysteinate)FeII(CN)(CO)2 Complex B from HydG to HydE. Angew. Chem.-Int. Ed. 62:e202314819. https://doi.org/10.1002/anie.202314819

Panek D, Pasieka A, Latacz G, Zaręba P, Szczęch M, Godyń J, Chantegreil F, Nachon F, Brazzolotto X, Skrzypczak-Wiercioch A, Walczak M, Smolik M, Sałat K, Höfner G, Wanner K, Więckowska A, Malawska B (2023) Discovery of new, highly potent and selective inhibitors of BuChE – design, synthesis. Eur. J. Med. Chem. 249:115135 https://doi.org/10.1016/j.ejmech.2023.115135

Bihani SC, Nagar V, Kumar M. (2023) Mechanistic and evolutionary insights into alkaline phosphatase superfamily through structure-function studies on Sphingomonas alkaline phosphatase. Arch. Biochem. Biophys. 736:109524 https://doi.org/10.1016/j.abb.2023.109524

Bui S, Gil-Guerrero S, van der Linden P, Carpentier P, Ceccarelli M, Jambrina PG, Steiner RA (2023) Evolutionary adaptation from hydrolytic to oxygenolytic catalysis at the α/β-hydrolase fold. Chem. Sci. 14, 10547-10560. https://doi.org/10.1039/d3sc03044j

Maranha A, Costa M, Ripoll-Rozada J, Manso JA, Miranda V, Mendes VM, Manadas B, Macedo-Ribeiro S, Ventura MR, Pereira PJB, Empadinhas N (2023) Self-recycling and partially conservative replication of mycobacterial methylmannose polysaccharides. Commun. Biol. 6:108, https://doi.org/10.1038/s42003-023-04448-3

Menke FS, Mazzier D, Wicher B, Allmendinger L, Kauffmann B, Maurizot V, Huc I (2023) Molecular torsion springs: alteration of helix curvature in frustrated tertiary folds. Organ. Biomol. Chem. 21, 1275-1283, https://doi.org/10.1039/d2ob02109a

Nóbrega CS, Carvalho AL, Romão MJ, Pauleta SR (2023) Structural Characterization of Neisseria gonorrhoeae Bacterial Peroxidase-Insights into the Catalytic Cycle of Bacterial Peroxidases. Int. J. Mol. Sci. 24:6246. https://doi.org/10.3390/ijms24076246

Pendem N, Cussol L, Didierjean C, Kauffmann B, Dolain C, Guichard G (2023) Synthesis and Crystallographic Characterization of Helical Hairpin Oligourea Foldamers. Chem.-Eur. J. 29: e202300087, https://doi.org/10.1002/chem.202300087

Rhimi M, Da Lage JL, Haser R, Feller G, Aghajari N (2023) Structural and Functional Characterization of Drosophila melanogaster α-Amylase. Molecules 28:5327 https://doi.org/10.3390/molecules28145327

Roehrig S, Ackerstaff J, Jiménez Núñez E, Teller H, Ellerbrock P, Meier K, Heitmeier S, Tersteegen A, Stampfuss J, Lang D, Schlemmer KH, Schaefer M, Gericke KM, Kinzel T, Meibom D, Schmidt M, Gerdes C, Follmann M, Hillisch A. (2023) Design and Preclinical Characterization Program toward Asundexian (BAY 2433334), an Oral Factor XIa Inhibitor for the Prevention and Treatment of Thromboembolic Disorders J. Med. Chem. 66, 12203-12224. https://doi.org/10.1021/acs.jmedchem.3c00795

Schwartz M, Perrot T, Beurton J, Zannini F, Morel-Rouhier M, Gelhaye E, Neiers F, Schaniel D, Favier F, Jacquot JP, Leroy P, Clarot I, Boudier A, Didierjean C (2023) Structural insights into the interactions of glutathione transferases with a nitric oxide carrier and sodium nitroprusside. Biochem. Biophys. Res. Commun. 649, 79-86, https://doi.org/10.1016/j.bbrc.2023.01.099

 

2022

Drago VN, Dajnowicz S, Parks JM, Blakeley MP, Keen DA, Coquelle N, Weiss KL, Gerlits O, Kovalevsky A, Mueser TC. An N⋯H⋯N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction. Chem. Sci. 13, 10057-10065. https://doi.org/10.1039/d2sc02285k

Mocchetti E., Morette L., Mulliert G., Mathiot S., Guillot B., Dehez F., Chauvat F., Cassier-Chauvat C., Brochier-Armanet C., Didierjean C., Hecker A. (2022) Biochemical and structural characterization of chi-class glutathione transferases: A snapshot on the glutathione transferase encoded by sll0067 gene in the cyanobacterium Synechocystis sp. Strain PCC 6803, Biomolecules 12,  1466, https://doi.org/10.3390/biom12101466

Neiers F., Gourrat K., Canon F., Schwartz M. (2022), Metabolism of cysteine conjugates and production of flavor sulfur compounds by a carbon-sulfur lyase from the oral anaerobe Fusobacterium nucleatum, Journal of Agricultural and Food Chemistry 70, 9969-9979,  https://doi.org/10.1021/acs.jafc.2c01727

Bihani SC, Gupta GD, Hosur MV (2022) Molecular basis for reduced cleavage activity and drug resistance in D30N HIV-1 protease. Journal of Biomolecular Structure and Dynamics, online ahead of print, https://doi.org/10.1080/07391102.2021.1982007

Collet L, Vander Wauven C, Oudjama Y, Galleni M, Dutoit R (2022) Highlighting the factors governing transglycosylation in the GH5_5 endo-1,4-β-glucanase RBcel1. Acta Crystallographica D Structural Biology 78, 278-289, https://doi.org/10.1107/S2059798321013541

Schulz EC, Yorke BA, Pearson AR, Mehrabi P (2022) Best practices for time-resolved serial synchrotron crystallography. Acta Crystallographica D Structural Biology 78, 14-29, https://doi.org/10.1107/S2059798321011621

Zannini F, Mathiot S, Couturier J., Didierjean C., Rouhier N (2022) Structural Insights into a Fusion Protein between a Glutaredoxin-like and a Ferredoxin-Disulfide Reductase Domain from an Extremophile Bacterium. Inorganics 10, 24, https://doi.org/10.3390/inorganics10020024

 

2021

Aggarwal S, von Wachenfeldt C, Fisher SZ, Oksanen E (2021) A protocol for production of perdeuterated OmpF porin for neutron crystallography. Protein Expression and Purification 188, 105954, https://doi.org/10.1016/j.pep.2021.105954

Atcher J., Mateus P., Kauffmann B., Rosu F., Maurizot V., Huc I. (2021) Large-Amplitude Conformational Changes in Self-Assembled Multi-Stranded Aromatic Sheets. Angewandte Chemie International Edition 60, 2574-2577, https://doi.org/10.1002/anie.202014670

Blum TB, Housset D, Clabbers MTB, van Genderen E, Bacia-Verloop M, Zander U, McCarthy AA, Schoehn G, Ling WL, Abrahams JP (2021) Statistically correcting dynamical electron scattering improves the refinement of protein nanocrystals, including charge refinement of coordinated metals. Acta Crystallographica D Structural Biology 77, 75-85, https://doi.org/10.1107/S2059798320014540

Chiari L, Carpentier P, Kieffer-Jaquinod S, Gogny A, Pérard J, Ravanel S, Cobessi D, Ménage S, Dumas R, Hamelin O (2021) LEAFY protein crystals with a honeycomb structure as a platform for selective preparation of outstanding stable bio-hybrid materials. Nanoscale 13, 8901-8908, https://doi.org/10.1039/d1nr00268f

Favier A, Gans P, Erba EB, Signor L, Muthukumar SS, Pfannschmidt T, Blanvillain R, Cobessi D (2021) The Plastid-encoded RNA polymerase-associated protein PAP9 is a superoxide dismutase with unusual structural features. Frontiers in Plant Science 12, 668897, https://doi.org/10.3389/fpls.2021.668897

Gajdos L, Blakeley MP, Kumar A, Wimmerová M, Haertlein M, Forsyth VT, Imberty A, Devos JM (2021) Visualization of hydrogen atoms in a perdeuterated lectin-fucose complex reveals key details of protein-carbohydrate interactions. Structure 29, 1003-1013, https://doi.org/10.1016/j.str.2021.03.003

Gupta D, Tiwari P, Haque MA, Sachdeva E, Hassan MI, Ethayathulla AS, Kaur P (2021) Structural insights into the transient closed conformation and pH dependent ATPase activity of S.Typhi GyraseB N- terminal domain. Archives of Biochemistry and Biophysics 701, 108786, https://doi.org/10.1016/j.abb.2021.108786

Jaho S, Junius N, Borel F, Sallaz-Damaz Y, Salmon JB, Budayova-Spano M (2021) Crystallization of Proteins on Chip by Microdialysis for In Situ X-ray Diffraction Studies. Journal of Visualized Experiments 170, e61660, https://doi.org/10.3791/61660

Kelpšas V, Caldararu O, Blakeley MP, Coquelle N, Wierenga RK, Ryde U, von Wachenfeldt C, Oksanen E (2021) Neutron structures of Leishmania mexicana triosephosphate isomerase in complex with reaction-intermediate mimics shed light on the proton-shuttling steps, IUCrJ 8, 633-643, https://doi.org/10.1107/S2052252521004619

Martínez-Alarcón D., Balloy V., Bouchara J.P., Pieters R.J., Varrot A. (2021) Biochemical and structural studies of target lectin SapL1 from the emerging opportunistic microfungus Scedosporium apiospermum. Scientific Reports 11, 16109, https://doi.org/10.1038/s41598-021-95008-4

McGregor L, Földes T, Bui S, Moulin M, Coquelle N, Blakeley MP, Rosta E, Steiner RA (2021) Joint neutron/X-ray crystal structure of a mechanistically relevant complex of perdeuterated urate oxidase and simulations provide insight into the hydration step of catalysis. IUCrJ 8, 46-59, https://doi.org/10.1107/S2052252520013615

Perrot T, Schwartz M, Deroy A, Girardet JM, Kohler A, Morel-Rouhier M, Favier F, Gelhaye E, Didierjean C (2021) Diversity of Omega Glutathione Transferases in mushroom-forming fungi revealed by phylogenetic, transcriptomic, biochemical and structural approaches Fungal Genetics and Biology 148, 103506, https://doi.org/10.1016/j.fgb.2020.103506

Roret T, Zhang B, Moseler A, Dhalleine T, Gao XH, Couturier J, Lemaire SD, Didierjean C, Johnson MK, Rouhier N (2021) Atypical iron-sulfur cluster binding, redox activity and structural properties of Chlamydomonas reinhardtii glutaredoxin 2. Antioxidants 10, 803, https://doi.org/10.3390/antiox10050803

Singh J, Maurya A, Singh PK, Viswanathan V, Ahmad MI, Sharma P, Sharma S, Singh TP (2021) A Peptide Bond from the Inter-lobe Segment in the Bilobal Lactoferrin Acts as a Preferred Site for Cleavage for Serine Proteases to Generate the Perfect C-lobe: Structure of the Pepsin Hydrolyzed Lactoferrin C-lobe at 2.28 Å Resolution. The Protein Journal 40, 857-866, https://doi.org/10.1007/s10930-021-10028-3

Sorigué D, Hadjidemetriou K, Blangy S, Gotthard G, Bonvalet A, Coquelle N, Samire P, Aleksandrov A, Antonucci L, Benachir A, Boutet S, Byrdin M, Cammarata M, Carbajo S, Cuiné S, Doak RB, Foucar L, Gorel A, Grünbein M, Hartmann E, Hienerwadel R, Hilpert M, Kloos M, Lane TJ, Légeret B, Legrand P, Li-Beisson Y, Moulin SLY, Nurizzo D, Peltier G, Schirò G, Shoeman RL, Sliwa M, Solinas X, Zhuang B, Barends TRM, Colletier JP, Joffre M, Royant A, Berthomieu C, Weik M, Domratcheva T, Brettel K, Vos MH, Schlichting I, Arnoux P, Müller P, Beisson F (2021) Mechanism and dynamics of fatty acid photodecarboxylase. Science 372, eabd5687, https://doi.org/10.1126/science.abd5687 [This article has been featured as a General News on the ESRF website on 08-04-2021: https://www.esrf.fr/home/news/general/content-news/general/green-chemistry-and-biofuel-the-mechanism-of-a-key-photoenzyme-decrypted.html and also belongs to the ESRF highlights 2021 booklet: https://www.esrf.fr/home/UsersAndScience/Publications/Highlights/esrf-highlights-2021.html]