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Michael G. Rossmann - One of the best experts on this subject based on the ideXlab platform.
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The structure determination of Sindbis virus core protein using Isomorphous Replacement and molecular Replacement averaging between two crystal forms.
Acta Crystallographica Section A Foundations of Crystallography, 1992Co-Authors: Liang Tong, Hok-kin Choi, Wladek Minor, Michael G. RossmannAbstract:The structure of Sindbis virus core protein has been determined by a combination of Multiple Isomorphous Replacement and molecular Replacement averaging techniques. The Multiple Isomorphous Replacement phase determinations were made for two crystal forms (P21 and P432~2 ) of the core protein. The real-space molecular Replacement averaging was subsequently carded out between two copies of the protein per asymmetric unit in the monoclinic form and one copy in the tetragonal form. This greatly improved the quality of the electron density maps. The Sindbis virus core protein polypeptide could be
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The structure determination of Sindbis virus core protein using Isomorphous Replacement and molecular Replacement averaging between two crystal forms.
Acta crystallographica. Section A Foundations of crystallography, 1992Co-Authors: Liang Tong, Hok-kin Choi, Wladek Minor, Michael G. RossmannAbstract:The structure of Sindbis virus core protein has been determined by a combination of Multiple Isomorphous Replacement and molecular Replacement averaging techniques. The Multiple Isomorphous Replacement phase determinations were made for two crystal forms (P2(1) and P4(3)2(1)2) of the core protein. The real-space molecular Replacement averaging was subsequently carried out between two copies of the protein per asymmetric unit in the monoclinic form and one copy in the tetragonal form. This greatly improved the quality of the electron density maps. The Sindbis virus core protein polypeptide could be traced and related to the known amino acid sequence. The averaging procedure between different crystal forms, as described in this paper, should be generally applicable to other systems.
Liang Tong - One of the best experts on this subject based on the ideXlab platform.
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The structure determination of Sindbis virus core protein using Isomorphous Replacement and molecular Replacement averaging between two crystal forms.
Acta Crystallographica Section A Foundations of Crystallography, 1992Co-Authors: Liang Tong, Hok-kin Choi, Wladek Minor, Michael G. RossmannAbstract:The structure of Sindbis virus core protein has been determined by a combination of Multiple Isomorphous Replacement and molecular Replacement averaging techniques. The Multiple Isomorphous Replacement phase determinations were made for two crystal forms (P21 and P432~2 ) of the core protein. The real-space molecular Replacement averaging was subsequently carded out between two copies of the protein per asymmetric unit in the monoclinic form and one copy in the tetragonal form. This greatly improved the quality of the electron density maps. The Sindbis virus core protein polypeptide could be
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The structure determination of Sindbis virus core protein using Isomorphous Replacement and molecular Replacement averaging between two crystal forms.
Acta crystallographica. Section A Foundations of crystallography, 1992Co-Authors: Liang Tong, Hok-kin Choi, Wladek Minor, Michael G. RossmannAbstract:The structure of Sindbis virus core protein has been determined by a combination of Multiple Isomorphous Replacement and molecular Replacement averaging techniques. The Multiple Isomorphous Replacement phase determinations were made for two crystal forms (P2(1) and P4(3)2(1)2) of the core protein. The real-space molecular Replacement averaging was subsequently carried out between two copies of the protein per asymmetric unit in the monoclinic form and one copy in the tetragonal form. This greatly improved the quality of the electron density maps. The Sindbis virus core protein polypeptide could be traced and related to the known amino acid sequence. The averaging procedure between different crystal forms, as described in this paper, should be generally applicable to other systems.
Hok-kin Choi - One of the best experts on this subject based on the ideXlab platform.
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The structure determination of Sindbis virus core protein using Isomorphous Replacement and molecular Replacement averaging between two crystal forms.
Acta Crystallographica Section A Foundations of Crystallography, 1992Co-Authors: Liang Tong, Hok-kin Choi, Wladek Minor, Michael G. RossmannAbstract:The structure of Sindbis virus core protein has been determined by a combination of Multiple Isomorphous Replacement and molecular Replacement averaging techniques. The Multiple Isomorphous Replacement phase determinations were made for two crystal forms (P21 and P432~2 ) of the core protein. The real-space molecular Replacement averaging was subsequently carded out between two copies of the protein per asymmetric unit in the monoclinic form and one copy in the tetragonal form. This greatly improved the quality of the electron density maps. The Sindbis virus core protein polypeptide could be
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The structure determination of Sindbis virus core protein using Isomorphous Replacement and molecular Replacement averaging between two crystal forms.
Acta crystallographica. Section A Foundations of crystallography, 1992Co-Authors: Liang Tong, Hok-kin Choi, Wladek Minor, Michael G. RossmannAbstract:The structure of Sindbis virus core protein has been determined by a combination of Multiple Isomorphous Replacement and molecular Replacement averaging techniques. The Multiple Isomorphous Replacement phase determinations were made for two crystal forms (P2(1) and P4(3)2(1)2) of the core protein. The real-space molecular Replacement averaging was subsequently carried out between two copies of the protein per asymmetric unit in the monoclinic form and one copy in the tetragonal form. This greatly improved the quality of the electron density maps. The Sindbis virus core protein polypeptide could be traced and related to the known amino acid sequence. The averaging procedure between different crystal forms, as described in this paper, should be generally applicable to other systems.
Wladek Minor - One of the best experts on this subject based on the ideXlab platform.
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The structure determination of Sindbis virus core protein using Isomorphous Replacement and molecular Replacement averaging between two crystal forms.
Acta Crystallographica Section A Foundations of Crystallography, 1992Co-Authors: Liang Tong, Hok-kin Choi, Wladek Minor, Michael G. RossmannAbstract:The structure of Sindbis virus core protein has been determined by a combination of Multiple Isomorphous Replacement and molecular Replacement averaging techniques. The Multiple Isomorphous Replacement phase determinations were made for two crystal forms (P21 and P432~2 ) of the core protein. The real-space molecular Replacement averaging was subsequently carded out between two copies of the protein per asymmetric unit in the monoclinic form and one copy in the tetragonal form. This greatly improved the quality of the electron density maps. The Sindbis virus core protein polypeptide could be
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The structure determination of Sindbis virus core protein using Isomorphous Replacement and molecular Replacement averaging between two crystal forms.
Acta crystallographica. Section A Foundations of crystallography, 1992Co-Authors: Liang Tong, Hok-kin Choi, Wladek Minor, Michael G. RossmannAbstract:The structure of Sindbis virus core protein has been determined by a combination of Multiple Isomorphous Replacement and molecular Replacement averaging techniques. The Multiple Isomorphous Replacement phase determinations were made for two crystal forms (P2(1) and P4(3)2(1)2) of the core protein. The real-space molecular Replacement averaging was subsequently carried out between two copies of the protein per asymmetric unit in the monoclinic form and one copy in the tetragonal form. This greatly improved the quality of the electron density maps. The Sindbis virus core protein polypeptide could be traced and related to the known amino acid sequence. The averaging procedure between different crystal forms, as described in this paper, should be generally applicable to other systems.
Georg E Schulz - One of the best experts on this subject based on the ideXlab platform.
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the structure of porin from rhodobacter capsulatus at 1 8 a resolution
FEBS Letters, 1991Co-Authors: M. S. Weiss, Jurgen Weckesser, A Kreusch, Emile Schiltz, Uwe Nestel, Wolfram Welte, Georg E SchulzAbstract:The structure of the porin from Rhodobacter capsulanus was determined at a resolution of 1.8 A. The analysis started from a closely related crystal structure that had been solved at a medium resolution of 3 A using Multiple Isomorphous Replacement and solvent flattening. The new structure contains the complete sequence of 301 amino acid residues. Refinement of the model is under way: the present R-factor is 22% with good geometry. Except for the lengths of several loops, the resulting chain fold corresponds to the medium resolution model. The membrane channel is lined by a large number of ionogenic side chains with characteristic segregation of differently charged groups.
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Structure of cyclodextrin glycosyltransferase refined at 2.0 A resolution.
Journal of molecular biology, 1991Co-Authors: Claudio Klein, Georg E SchulzAbstract:Abstract The previously reported structural model of cyclodextrin glycosyltransferase (EC 2.4.1.19) from Bacillus circulans has been improved. For this purpose the known sequence was built into an electron density map established by Multiple Isomorphous Replacement and subsequent solvent-flattening at 2.5 A resolution. The resulting model was refined at 2.0 A resolution using a simulated annealing refinement method. Based on 70,171 independent reflections in the range 7.0 to 2.0 A resolution, a final R-factor of 17.6% was obtained with a model obeying standard geometry within 0.013 A in bond lengths and 2.7 ° in bond angles. The final model consists of all 684 amino acid residues, two calcium ions and 588 solvent molecules.
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The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 Å resolution
Proteins, 1991Co-Authors: Ulrich Ermler, Georg E SchulzAbstract:The structure of glutathione reductase from Escherichia coli has been solved at 3 A resolution using Multiple Isomorphous Replacement, solvent flattening, and molecular Replacement on the basis of the homologous (53% identical residues) and structurally well-established human enzyme. The structures of both enzyme species agree with each other in a global way; there is no domain rearrangement. In detail, clear structural differences can be observed. The structure analysis of the E. coli enzyme was tackled in order to understand site-directed mutants, the most spectacular of which changed the cofactor specificity of this enzyme from NADP to NAD (Scrutton et al., 1990, Nature 343:38-43).