ArticleActa crystallographica. Section F, Structural biology and crystallization communications2008
Preliminary time-of-flight neutron diffraction study of human deoxyhemoglobin.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Protonation states of histidine and other key residues in deoxy normal human adult hemoglobin by neutron protein crystallography.Acta crystallographica. Section D, Biological crystallography · 2010Article
- Hemoglobin redux: combining neutron and X-ray diffraction with mass spectrometry to analyse the quaternary state of oxidized hemoglobins.Acta crystallographica. Section D, Biological crystallography · 2010Article
- Macromolecular neutron crystallography at the Protein Crystallography Station (PCS).Acta crystallographica. Section D, Biological crystallography · 2010Article
- Preliminary neutron and X-ray crystallographic studies of equine cyanomethemoglobin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- A preliminary neutron diffraction study of gamma-chymotrypsin.Acta crystallographica. Section F, Structural biology and crystallization communications · 2009Article
- Neutron crystallography: opportunities, challenges, and limitations.Current opinion in structural biology · 2008Review
- Protein structures by spallation neutron crystallography.Journal of synchrotron radiation · 2008Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
Abstract
Human hemoglobin (HbA) is an intricate system that has evolved to efficiently transport oxygen molecules (O(2)) from lung to tissue. Its quaternary structure can fluctuate between two conformations, T (tense or deoxy) and R (relaxed or oxy), which have low and high affinity for O(2), respectively. The binding of O(2) to the heme sites of HbA is regulated by protons and by inorganic anions. In order to investigate the role of the protonation states of protein residues in O(2) binding, large crystals of deoxy HbA (approximately 20 mm(3)) were grown in D(2)O under anaerobic conditions for neutron diffraction studies. A time-of-flight neutron data set was collected to 1.8 A resolution on the Protein Crystallography Station (PCS) at the spallation source run by Los Alamos Neutron Science Center (LANSCE). The HbA tetramer (64.6 kDa; 574 residues excluding the four heme groups) occupies the largest asymmetric unit (space group P2(1)) from which a high-resolution neutron data set has been collected to date.
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Registered trials
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