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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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DOI no:
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Acta Crystallogr D Biol Crystallogr
59:982-988
(2003)
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PubMed id:
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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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A.E.Miele,
L.Federici,
G.Sciara,
F.Draghi,
M.Brunori,
B.Vallone.
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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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Selected figure(s)
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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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Figure was
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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D.A.Kondrashov,
W.Zhang,
R.Aranda,
B.Stec,
and
G.N.Phillips
(2008).
Sampling of the native conformational ensemble of myoglobin via structures in different crystalline environments.
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Proteins,
70,
353-362.
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PDB codes:
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T.Kinoshita,
R.Maruki,
M.Warizaya,
H.Nakajima,
and
S.Nishimura
(2005).
Structure of a high-resolution crystal form of human triosephosphate isomerase: improvement of crystals using the gel-tube method.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
61,
346-349.
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PDB code:
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S.V.Lynch,
E.L.Brodie,
A.Matin,
and
A.Matin
(2004).
Role and regulation of sigma S in general resistance conferred by low-shear simulated microgravity in Escherichia coli.
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J Bacteriol,
186,
8207-8212.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
