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Instruments / Technical Area	Publication Details	Published	Actions
B21-High Throughput SAXS	Isolation and characterization of monomeric human RAD51: a novel tool for investigating homologous recombination in cancer Francesco Rinaldi , Fabrizio Schipani , Beatrice Balboni , Federico Catalano , Roberto Marotta , Samuel H. Myers , Viola Previtali , Marina Veronesi , Luigi Scietti , Valentina Cecatiello , Sebastiano Pasqualato , Jose Antonio Ortega , Stefania Girotto , Andrea Cavalli Angewandte Chemie International Edition DOI: 10.1002/anie.202312517 Diamond Proposal Number(s): [30465] Open Access Show Abstract ▼ Abstract: RAD51 is a key player in the homologous recombination pathway. Upon DNA damage, RAD51 is transported into the nucleus by BRCA2, where it can repair DNA double-strand breaks. Due to the structural complexity and dynamics, researchers have not yet clarified the mechanistic details of every step of RAD51 recruitment and DNA repair. RAD51 possesses an intrinsic tendency to form oligomeric structures, which make it challenging to conduct biochemical and biophysical investigations. Here, for the first time, we report on the isolation and characterization of a human monomeric RAD51 recombinant form, obtained through a double mutation, which preserves the protein’s integrity and functionality. We investigated different buffers to identify the most suitable condition needed to definitively stabilize the monomer. The monomer of human RAD51 provides the community with a unique biological tool for investigating RAD51-mediated homologous recombination, and paves the way for more reliable structural, mechanistic, and drug discovery studies.	Nov 2023
Krios III-Titan Krios III at Diamond	High-light versus low-light: Effects on paired photosystem II supercomplex structural rearrangement in pea plants Alessandro Grinzato , Pascal Albanese , Roberto Marotta , Paolo Swuec , Guido Saracco , Martino Bolognesi , Giuseppe Zanotti , Cristina Pagliano International Journal Of Molecular Sciences 21 DOI: 10.3390/ijms21228643 Diamond Proposal Number(s): [19714] Open Access Show Abstract ▼ Abstract: In plant grana thylakoid membranes Photosystem II (PSII) associates with a variable number of antenna proteins (LHCII) to form different types of supercomplexes (PSII-LHCII), whose organization is dynamically adjusted in response to light cues, with the C2S2 more abundant in high-light and the C2S2M2 in low-light. Paired PSII-LHCII supercomplexes interacting at their stromal surface from adjacent thylakoid membranes were previously suggested to mediate grana stacking. Here, we present the cryo-electron microscopy maps of paired C2S2 and C2S2M2 supercomplexes isolated from pea plants grown in high-light and low-light, respectively. These maps show a different rotational offset between the two supercomplexes in the pair, responsible for modifying their reciprocal interaction and energetic connectivity. This evidence reveals a different way by which paired PSII-LHCII supercomplexes can mediate grana stacking at diverse irradiances. Electrostatic stromal interactions between LHCII trimers almost completely overlapping in the paired C2S2 can be the main determinant by which PSII-LHCII supercomplexes mediate grana stacking in plants grown in high-light, whereas the mutual interaction of stromal N-terminal loops of two facing Lhcb4 subunits in the paired C2S2M2 can fulfil this task in plants grown in low-light. The high-light induced accumulation of the Lhcb4.3 protein in PSII-LHCII supercomplexes has been previously reported. Our cryo-electron microscopy map at 3.8 Å resolution of the C2S2 supercomplex isolated from plants grown in high-light suggests the presence of the Lhcb4.3 protein revealing peculiar structural features of this high-light-specific antenna important for photoprotection.	Nov 2020

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