3A38
Crystal structure of high-potential iron-sulfur protein from Thermochromatium tepidum at 0.7 angstrom resolution
Summary for 3A38
| Entry DOI | 10.2210/pdb3a38/pdb |
| Related | 1EYT 1IUA 3A39 |
| Descriptor | High-potential iron-sulfur protein, IRON/SULFUR CLUSTER, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | iron-sulfur cluster, electron transport, iron, iron-sulfur, metal-binding, transport |
| Biological source | Thermochromatium tepidum (Chromatium tepidum) |
| Total number of polymer chains | 1 |
| Total formula weight | 9525.77 |
| Authors | Takeda, K.,Kusumoto, K.,Hirano, Y.,Miki, K. (deposition date: 2009-06-10, release date: 2010-01-26, Last modification date: 2023-11-01) |
| Primary citation | Takeda, K.,Kusumoto, K.,Hirano, Y.,Miki, K. Detailed assessment of X-ray induced structural perturbation in a crystalline state protein. J.Struct.Biol., 169:135-144, 2010 Cited by PubMed Abstract: The positions of hydrogen atoms significantly define protein functions. However, such information from protein crystals is easily disturbed by X-rays. The damage can not be prevented completely even in the data collection at cryogenic temperatures. Therefore, the influence of X-rays should be precisely estimated in order to derive meaningful information from the crystallographic results. Diffraction data from a single crystal of the high-potential iron-sulfur protein (HiPIP) from Thermochromatium tepidum were collected at an undulator beamline of a third generation synchrotron facility, and were merged into three data sets according to X-ray dose. A series of structures analyzed at 0.70A shows detailed views of the X-ray induced perturbation, such as the positional changes of hydrogen atoms of a water molecule. Based on the results, we successfully collected a low perturbation data set using attenuated X-rays. There was no influence on the crystallographic statistics, such as the relative B factors, during the course of data collection. The electron densities for hydrogen atoms were more clear despite the slightly lower resolution. PubMed: 19782139DOI: 10.1016/j.jsb.2009.09.012 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (0.7 Å) |
Structure validation
Download full validation report
