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Victoria N. Drago
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Imaging active site chemistry and protonation states: NMR crystallography of the tryptophan synthase α-aminoacrylate intermediate
JB Holmes, V Liu, BG Caulkins, E Hilario, RK Ghosh, VN Drago, ...
Proceedings of the National Academy of Sciences 119 (2), e2109235119, 2022
272022
Pyridoxal 5′-phosphate dependent reactions: analyzing the mechanism of aspartate aminotransferase
TC Mueser, V Drago, A Kovalevsky, S Dajnowicz
Methods in enzymology 634, 333-359, 2020
132020
Synthesis and in Vitro Characterization of Trehalose‐Based Inhibitors of Mycobacterial Trehalose 6‐Phosphate Phosphatases
S Kapil, C Petit, VN Drago, DR Ronning, SJ Sucheck
ChemBioChem 20 (2), 260-269, 2019
132019
Microgravity crystallization of perdeuterated tryptophan synthase for neutron diffraction
VN Drago, JM Devos, MP Blakeley, VT Forsyth, AY Kovalevsky, CA Schall, ...
npj Microgravity 8 (1), 13, 2022
62022
An N⋯ H⋯ N low-barrier hydrogen bond preorganizes the catalytic site of aspartate aminotransferase to facilitate the second half-reaction
VN Drago, S Dajnowicz, JM Parks, MP Blakeley, DA Keen, N Coquelle, ...
Chemical Science 13 (34), 10057-10065, 2022
62022
Neutron diffraction from a microgravity-grown crystal reveals the active site hydrogens of the internal aldimine form of tryptophan synthase
VN Drago, JM Devos, MP Blakeley, VT Forsyth, JM Parks, A Kovalevsky, ...
Cell Reports Physical Science, 2024
2024
Revealing protonation states and tracking substrate in serine hydroxymethyltransferase with room-temperature X-ray and neutron crystallography
VN Drago, C Campos, M Hooper, A Collins, O Gerlits, KL Weiss, ...
Communications Chemistry 6 (1), 162, 2023
2023
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