1n9h: Difference between revisions

Revision as of 00:55, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1n9h.png

Template:STRUCTURE 1n9h

structure of microgravity-grown oxidized myoglobin mutant YQR (ISS6A)structure of microgravity-grown oxidized myoglobin mutant YQR (ISS6A)

Template:ABSTRACT PUBMED 12777759

About this StructureAbout this Structure

1N9H is a Single protein structure of sequence from Physeter catodon. Full crystallographic information is available from OCA.

ReferenceReference

Analysis of the effect of microgravity on protein crystal quality: the case of a myoglobin triple mutant., Miele AE, Federici L, Sciara G, Draghi F, Brunori M, Vallone B, Acta Crystallogr D Biol Crystallogr. 2003 Jun;59(Pt 6):982-8. Epub 2003, May 23. PMID:12777759

Page seeded by OCA on Tue Jul 29 00:55:12 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''structure of microgravity-grown oxidized myoglobin mutant YQR (ISS6A)'''
+===structure of microgravity-grown oxidized myoglobin mutant YQR (ISS6A)===
-==Overview==
+<!--
-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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12777759}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12777759 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12777759}}
 ==About this Structure==
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