Summary for 6QE4
| Entry DOI | 10.2210/pdb6qe4/pdb |
| Descriptor | Putative transferase CAF17, mitochondrial, 5-amino-2,4,6-triiodobenzene-1,3-dicarboxylic acid (3 entities in total) |
| Functional Keywords | mitochondrial protein, fe-s protein biogenesis, infantile leukodystrophy, i3c phasing., protein binding |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 37202.41 |
| Authors | Calderone, V.,Ciofi-Baffoni, S.,Gourdoupis, S.,Banci, L.,Nasta, V. (deposition date: 2019-01-04, release date: 2019-03-13, Last modification date: 2024-05-15) |
| Primary citation | Gourdoupis, S.,Nasta, V.,Ciofi-Baffoni, S.,Banci, L.,Calderone, V. In-house high-energy-remote SAD phasing using the magic triangle: how to tackle the P1 low symmetry using multiple orientations of the same crystal of human IBA57 to increase the multiplicity. Acta Crystallogr D Struct Biol, 75:317-324, 2019 Cited by PubMed Abstract: This article describes the approach used to solve the structure of human IBA57 in-house by 5-amino-2,4,6-triiodoisophthalic acid (I3C) high-energy-remote single-wavelength anomalous dispersion (SAD) phasing. Multiple orientations of the same triclinic crystal were exploited to acquire sufficient real data multiplicity for phasing. How the collection of an in-house native data set and its joint use with the I3C derivative through a SIRAS approach decreases the data multiplicity needed by almost 50% is described. Furthermore, it is illustrated that there is a clear data-multiplicity threshold value for success and failure in phasing, and how adding further data does not significantly affect substructure solution and model building. To our knowledge, this is the only structure present in the PDB that has been solved in-house by remote SAD phasing in space group P1 using only one crystal. All of the raw data used, derived from the different orientations, have been uploaded to Zenodo in order to enable software developers to improve methods for data processing and structure solution, and for educational purposes. PubMed: 30950402DOI: 10.1107/S2059798319000214 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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