Location of haem in bacterioferritin of E. coli
. A low‐resolution partial structure of bacterioferritin was solved using a combination of molecular replacement and rigid‐body refinement methods. Modification of bacterioferritin crystals by soaking in tetrachloroplatinate results in a phase transition from tetragonal symmetry (space group P42212)...
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| Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 1993-11, Vol.49 (6), p.597-600 |
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| container_title | Acta crystallographica. Section D, Biological crystallography. |
| container_volume | 49 |
| creator | Frolow, F. Kalb (Gilboa), A. J. Yariv, J. |
| description | . A low‐resolution partial structure of bacterioferritin was solved using a combination of molecular replacement and rigid‐body refinement methods. Modification of bacterioferritin crystals by soaking in tetrachloroplatinate results in a phase transition from tetragonal symmetry (space group P42212) to a pseudo‐cubic one (approximate space group I432). Helical parts of human H ferritin structure stripped of side chains beyond the Cβ atoms were used as the model. An electron‐density map of the refined model revealed a region of extended density which by its shape and position in a pocket between helices was identified as haem. Inclusion of haem in the refinement showed that it can occupy only one of two symmetry‐related sites near a twofold axis of the molecule. |
| doi_str_mv | 10.1107/S0907444993007073 |
| format | Article |
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J. ; Yariv, J.</creator><creatorcontrib>Frolow, F. ; Kalb (Gilboa), A. J. ; Yariv, J.</creatorcontrib><description>. A low‐resolution partial structure of bacterioferritin was solved using a combination of molecular replacement and rigid‐body refinement methods. Modification of bacterioferritin crystals by soaking in tetrachloroplatinate results in a phase transition from tetragonal symmetry (space group P42212) to a pseudo‐cubic one (approximate space group I432). Helical parts of human H ferritin structure stripped of side chains beyond the Cβ atoms were used as the model. An electron‐density map of the refined model revealed a region of extended density which by its shape and position in a pocket between helices was identified as haem. Inclusion of haem in the refinement showed that it can occupy only one of two symmetry‐related sites near a twofold axis of the molecule.</description><identifier>ISSN: 1399-0047</identifier><identifier>ISSN: 0907-4449</identifier><identifier>EISSN: 1399-0047</identifier><identifier>DOI: 10.1107/S0907444993007073</identifier><identifier>PMID: 15299499</identifier><language>eng</language><publisher>5 Abbey Square, Chester, Cheshire CH1 2HU, England: International Union of Crystallography</publisher><subject>Analytical, structural and metabolic biochemistry ; Biological and medical sciences ; Crystalline structure ; Fundamental and applied biological sciences. Psychology ; Hemoproteins ; Metalloproteins ; Molecular biophysics ; Proteins ; Structure in molecular biology</subject><ispartof>Acta crystallographica. 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Inclusion of haem in the refinement showed that it can occupy only one of two symmetry‐related sites near a twofold axis of the molecule.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Biological and medical sciences</subject><subject>Crystalline structure</subject><subject>Fundamental and applied biological sciences. 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Section D, Biological crystallography.</jtitle><addtitle>Acta Cryst. D</addtitle><date>1993-11</date><risdate>1993</risdate><volume>49</volume><issue>6</issue><spage>597</spage><epage>600</epage><pages>597-600</pages><issn>1399-0047</issn><issn>0907-4449</issn><eissn>1399-0047</eissn><abstract>. A low‐resolution partial structure of bacterioferritin was solved using a combination of molecular replacement and rigid‐body refinement methods. Modification of bacterioferritin crystals by soaking in tetrachloroplatinate results in a phase transition from tetragonal symmetry (space group P42212) to a pseudo‐cubic one (approximate space group I432). Helical parts of human H ferritin structure stripped of side chains beyond the Cβ atoms were used as the model. An electron‐density map of the refined model revealed a region of extended density which by its shape and position in a pocket between helices was identified as haem. 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| ispartof | Acta crystallographica. Section D, Biological crystallography., 1993-11, Vol.49 (6), p.597-600 |
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| source | Crystallography Journals Online |
| subjects | Analytical, structural and metabolic biochemistry Biological and medical sciences Crystalline structure Fundamental and applied biological sciences. Psychology Hemoproteins Metalloproteins Molecular biophysics Proteins Structure in molecular biology |
| title | Location of haem in bacterioferritin of E. coli |
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