6HEF
Room temperature structure of the (SR)Ca2+-ATPase Ca2-E1-CaAMPPCP form
Summary for 6HEF
| Entry DOI | 10.2210/pdb6hef/pdb |
| Descriptor | Sarcoplasmic/endoplasmic reticulum calcium ATPase 1, PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER, CALCIUM ION, ... (5 entities in total) |
| Functional Keywords | sarcoplasmic/endoplasmic reticulum calcium atpase 1a, hydrolase |
| Biological source | Oryctolagus cuniculus |
| Total number of polymer chains | 1 |
| Total formula weight | 111054.24 |
| Authors | Hjorth-Jensen, S.,Sorensen, T.L.M.,Oksanen, E.,Andersen, J.L.,Olesen, C.,Moller, J.V.,Nissen, P. (deposition date: 2018-08-20, release date: 2018-08-29, Last modification date: 2024-01-17) |
| Primary citation | Sorensen, T.L.M.,Hjorth-Jensen, S.J.,Oksanen, E.,Andersen, J.L.,Olesen, C.,Moller, J.V.,Nissen, P. Membrane-protein crystals for neutron diffraction. Acta Crystallogr D Struct Biol, 74:1208-1218, 2018 Cited by PubMed Abstract: Neutron 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. PubMed: 30605135DOI: 10.1107/S2059798318012561 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.538 Å) |
Structure validation
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