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The structure of Synechococcus elongatus enolase reveals key aspects of phosphoenolpyruvate binding.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2022, v. 78, n. 4, p. 177, doi. 10.1107/S2053230X22003612
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Conformational changes on substrate binding revealed by structures of Methylobacterium extorquens malate dehydrogenase.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2018, v. 74, n. 10, p. 610, doi. 10.1107/S2053230X18011809
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Structure of Methylobacterium extorquens malyl-CoA lyase: CoA-substrate binding correlates with domain shift.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2017, v. 73, n. 2, p. 79, doi. 10.1107/S2053230X17001029
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Neutron and high-resolution room-temperature X-ray data collection from crystallized lytic polysaccharide monooxygenase.
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- Acta Crystallographica: Section F, Structural Biology Communications, 2015, v. 71, n. 11, p. 1448, doi. 10.1107/S2053230X15019743
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Backbone and side chain chemical shift assignment of diisopropyl fluorophosphatase (DFPase) from Loligo vulgaris, an organophosphorus-degrading enzyme.
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- Biomolecular NMR Assignments, 2023, v. 17, n. 1, p. 55, doi. 10.1007/s12104-023-10120-y
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Neutron Crystallography for the Study of Hydrogen Bonds in Macromolecules.
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- Molecules, 2017, v. 22, n. 4, p. 596, doi. 10.3390/molecules22040596
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Energy optimization of a regular macromolecular crystallography beamline for ultra-high-resolution crystallography.
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- Journal of Synchrotron Radiation, 2015, v. 22, n. 1, p. 172, doi. 10.1107/S1600577514022619
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