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pubmed-article:11914507pubmed:abstractTextThe three-dimensional structure of recombinant haemoglobin from the trematode Paramphistomum epiclitum, displaying the highest oxygen affinity so far observed for (non)vertebrate haemoglobins, has previously been determined at 1.17 A resolution (orthorhombic space group P2(1)2(1)2(1)). In the present communication, the three-dimensional structure of wild-type P. epiclitum haemoglobin is reported at 1.85 A resolution in a monoclinic crystal form (R factor = 16.1%, R(free) = 22.0%). Comparison of P. epiclitum (recombinant versus wild-type ferric Hb) structures in the two crystal forms shows structural differences in the haem proximal and distal sites which have not been reported for other known haemoglobin structures previously.lld:pubmed
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pubmed-article:11914507pubmed:authorpubmed-author:BolognesiMart...lld:pubmed
pubmed-article:11914507pubmed:authorpubmed-author:AscenziPaoloPlld:pubmed
pubmed-article:11914507pubmed:authorpubmed-author:MoensLucLlld:pubmed
pubmed-article:11914507pubmed:authorpubmed-author:MilaniMarioMlld:pubmed
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pubmed-article:11914507pubmed:authorpubmed-author:DewildeSylvia...lld:pubmed
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pubmed-article:11914507pubmed:volume58lld:pubmed
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pubmed-article:11914507pubmed:pagination719-22lld:pubmed
pubmed-article:11914507pubmed:dateRevised2007-7-24lld:pubmed
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pubmed-article:11914507pubmed:year2002lld:pubmed
pubmed-article:11914507pubmed:articleTitleStructural plasticity in the eight-helix fold of a trematode haemoglobin.lld:pubmed
pubmed-article:11914507pubmed:affiliationDepartment of Physics-INFM, Advanced Biotechnology Centre, University of Genova, Largo Rosanna Benzi 10, I-16146 Genova, Italy.lld:pubmed
pubmed-article:11914507pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11914507pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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