1thb
From Proteopedia
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'''REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION''' | '''REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION''' | ||
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[[Category: Liddington, R C.]] | [[Category: Liddington, R C.]] | ||
[[Category: Waller, D A.]] | [[Category: Waller, D A.]] | ||
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- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:56:53 2008'' | |
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Revision as of 06:56, 3 May 2008
REFINEMENT OF A PARTIALLY OXYGENATED T STATE HAEMOGLOBIN AT 1.5 ANGSTROMS RESOLUTION
Overview
The degree of ligation of T state human haemoglobin crystals is reduced by inositol hexaphosphate (IHP). The structure of a partially ligated haemoglobin has been refined using fast Fourier restrained-least-squares techniques. Manual interventions were required to escape from local minima and introduce a large number of solvent molecules. Individual isotropic temperature factors were refined for all atoms and the final average atomic temperature factor is 32.3 A2. The final R factor is 19.6% for all data between 10 and 1.5 A. The final model consists of 4560 protein atoms and 313 solvent molecules. The occupancies of the ligand atoms and the anisotropic behaviour of the iron atoms have been refined, demonstrating that the alpha haem groups are only partially ligated and that there is no ligation of the beta haems. Density for the IHP indicates that it is not well ordered even though changes in the ligation and structure of the haemoglobin indicate its presence.
About this Structure
1THB is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Refinement of a partially oxygenated T state human haemoglobin at 1.5 A resolution., Waller DA, Liddington RC, Acta Crystallogr B. 1990 Jun 1;46 ( Pt 3):409-18. PMID:2383372 Page seeded by OCA on Sat May 3 09:56:53 2008