Laura Gabriella Calmanovici Pacoste

All Publications

• Tracking the redox reaction of the iron enzyme ribonucleotide reductase using continuous SerialED and SFX STRUCTURE Pacoste, L., Kumar, R., Srinivas, V., Makita, H., Simon, P. S., Bannerjee, R., Minnetian, N. M., Bhowmick, A., Paley, D. W., Mittan-Moreau, D. W., Chatterjee, K., Rosenberg, D. J., Batyuk, A., Gee, L. B., Alonso-Mori, R., Sauter, N. K., Yano, J., Yachandra, V. K., John, J., Aurelius, O., Brewster, A. S., Kern, J. F., Blomberg, B., Lebrette, H., Xu, H., Hofer, G., Hogbom, M., Zou, X. 2026; 34 (6): 901-914

  Abstract

  Serial femtosecond crystallography (SFX) and continuous serial electron diffraction (c-SerialED) both enable high-resolution structure determination from protein microcrystals with minimal radiation damage, making it ideal for studying redox-active metalloenzymes. Here, c-SerialED and SFX were used to solve structures of the class Ia ribonucleotide reductase R2 subunit in oxidized (FeIII-FeIII), reduced (FeII-FeII), and re-oxidized states at ∼1.8 Å resolution, capturing three points in a redox reaction. These results demonstrate that c-SerialED can track reversible changes at the redox-site, enabling future time-resolved studies. Comparison between c-SerialED structures and SFX diffraction and emission data confirmed minimal radiation damage. Furthermore, previously reported structures use mercury in the crystallization condition and show mercury-induced conformational changes. Here, we use mercury-free crystallization conditions and reveal a water molecule in the redox center of the reduced state, absent in the previous structures, making these structures more representative of the physiological state.

  View details for DOI 10.1016/j.str.2026.03.006

  View details for Web of Science ID 001793387000001

  View details for PubMedID 42097140

  View details for PubMedCentralID PMC13166098