36OR
Room-temperature multiconformer model of HRas-GMPPNP
Summary for 36OR
| Entry DOI | 10.2210/pdb36or/pdb |
| Descriptor | GTPase HRas, CALCIUM ION, MAGNESIUM ION, ... (6 entities in total) |
| Functional Keywords | small gtpase, oncoprotein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 19625.28 |
| Authors | |
| Primary citation | Wang, H.K.,Greisman, J.B.,Dalton, K.M.,Hewitt, R.A.,White, K.I.,Hekstra, D.R. Symmetry Breaking under Vectorial Perturbations in Macromolecular X-ray Crystallography. Biorxiv, 2026 Cited by PubMed Abstract: Proteins are molecular machines whose dynamics govern their function. Using time-resolved crystallography, the basis of protein mechanics can be uncovered by physical perturbation on protein crystals. Perturbations are often vector fields that, in crystals, break symmetry. Lacking existing tools for analyzing symmetry breaking, we built open-source software to do so. We applied this method to three time-resolved crystallography experiments and analyzed the effect of vectorial perturbations on macromolecular crystal structure. We demonstrate that our method can handle symmetry reduction in all 65 Sohncke space groups. PubMed: 42856210DOI: 10.64898/2026.09.28.753211 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
Download full validation report
