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Room temperature structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP formRoom temperature structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP form
Structural highlights
Function[AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). Publication Abstract from PubMedNeutron macromolecular crystallography (NMX) has the potential to provide the experimental input to address unresolved aspects of transport mechanisms and protonation in membrane proteins. However, despite this clear scientific motivation, the practical challenges of obtaining crystals that are large enough to make NMX feasible have so far been prohibitive. Here, the potential impact on feasibility of a more powerful neutron source is reviewed and a strategy for obtaining larger crystals is formulated, exemplified by the calcium-transporting ATPase SERCA1. The challenges encountered at the various steps in the process from crystal nucleation and growth to crystal mounting are explored, and it is demonstrated that NMX-compatible membrane-protein crystals can indeed be obtained. Membrane-protein crystals for neutron diffraction.,Sorensen TLM, Hjorth-Jensen SJ, Oksanen E, Andersen JL, Olesen C, Moller JV, Nissen P Acta Crystallogr D Struct Biol. 2018 Dec 1;74(Pt 12):1208-1218. doi:, 10.1107/S2059798318012561. Epub 2018 Nov 30. PMID:30605135[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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