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PDBsum entry 1n9h
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Oxygen storage/transport
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PDB id
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1n9h
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutant.
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Authors
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A.E.Miele,
L.Federici,
G.Sciara,
F.Draghi,
M.Brunori,
B.Vallone.
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Ref.
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Acta Crystallogr D Biol Crystallogr, 2003,
59,
982-988.
[DOI no: ]
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PubMed id
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Abstract
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Crystals of the Met derivative of the sperm whale myoglobin triple mutant Mb-YQR
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.
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Figure 3.
Figure 3 Close up of the haem pocket Mb-YQR at 1.04 Å from the
ISS 8A mission. The hydrogen-bond network in the distal pocket
and the iron distances to the 5th and 6th coordination positions
are highlighted.
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The above figure is
reprinted
by permission from the IUCr:
Acta Crystallogr D Biol Crystallogr
(2003,
59,
982-988)
copyright 2003.
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