1N9X

structure of microgravity-grown oxidized myoglobin mutant YQR (ISS8A)

Summary for 1N9X

• Entry DOI: 10.2210/pdb1n9x/pdb
• Related: 1n9f 1n9h 1n9i 1naz
• Descriptor: Myoglobin, HYDROXIDE ION, SULFATE ION, ... (5 entities in total)
• Functional Keywords: globin fold, microgravity, oxygen storage-transport complex, oxygen storage/transport
• Biological source: Physeter catodon (sperm whale)
• Total number of polymer chains: 1
• Total formula weight: 18286.87

Authors

Miele, A.E.,Sciara, G.,Federici, L.,Draghi, F.,Brunori, M.,Vallone, B. (deposition date: 2002-11-26, 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

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: 12777759
DOI: 10.1107/S0907444903005924

Experimental method

X-RAY DIFFRACTION (1.6 Å)