1N9F
Structure of earth-grown oxidized Myoglobin mutant YQR (ISS6A)
Summary for 1N9F
| Entry DOI | 10.2210/pdb1n9f/pdb |
| Related | 1n9h 1n9i 1n9x 1naz |
| Descriptor | Myoglobin, HYDROXIDE ION, SULFATE ION, ... (5 entities in total) |
| Functional Keywords | globin fold, oxygen storage-transport complex, oxygen storage/transport |
| Biological source | Physeter catodon (sperm whale) |
| Total number of polymer chains | 1 |
| Total formula weight | 18190.81 |
| Authors | Miele, A.E.,Sciara, G.,Federici, L.,Vallone, B.,Brunori, M. (deposition date: 2002-11-25, release date: 2003-06-10, Last modification date: 2023-08-16) |
| Primary citation | Miele, A.E.,Federici, L.,Sciara, G.,Draghi, F.,Brunori, M.,Vallone, B. Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutant. Acta Crystallogr.,Sect.D, 59:982-988, 2003 Cited by PubMed Abstract: Crystals of the Met derivative of the sperm whale myoglobin triple mutant Mb-YQR [L(B10)Y, H(E7)Q and T(E10)R] were grown under microgravity conditions and on earth by vapour diffusion. A comparison of crystal quality after complete data collection and processing shows how microgravity-grown crystals diffract to better resolution and lead to considerably improved statistics for X-ray diffraction data compared with crystals grown on earth under the same conditions. The same set of experiments was reproduced on two different Spacelab missions (ISS 6A and ISS 8A) in 2001 and 2002. The structure of this mutant myoglobin, refined using data collected at ELETTRA (Trieste, Italy) from both kinds of crystals, shows that X-ray diffraction from microgravity-grown crystals leads to better defined electron-density maps as well as improved geometrical quality of the refined model. Improvement of the stereochemical parameters of a protein structure is fundamental to quantitative analysis of its function and dynamics and hence to thorough understanding of the molecular mechanisms of action. PubMed: 12777759DOI: 10.1107/S0907444903005924 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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