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Combining X-ray and electron-microscopy data to solve crystal structures.

Navaza J - Acta Crystallogr. D Biol. Crystallogr. (2007)

Bottom Line: Low-resolution electron-microscopy reconstructions can be used as search models in molecular replacement or may be combined with existing monomeric structures in order to produce multimeric models suitable for molecular replacement.The technique is described in the case of viral and subviral particles as well as in the case of oligomeric proteins.

View Article: PubMed Central - HTML - PubMed

Affiliation: Laboratoire de Microscopie Electronique Structurale, Institut de Biologie Structurale Jean-Pierre Ebel, 41 Rue Jules Horowitz, F-38027 Grenoble, France. jorge.navaza@ibs.fr

ABSTRACT
Low-resolution electron-microscopy reconstructions can be used as search models in molecular replacement or may be combined with existing monomeric structures in order to produce multimeric models suitable for molecular replacement. The technique is described in the case of viral and subviral particles as well as in the case of oligomeric proteins.

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Fit of the VP2 trimers into the cryo-TEM reconstruction of the T = 13 viral particle.
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fig4: Fit of the VP2 trimers into the cryo-TEM reconstruction of the T = 13 viral particle.

Mentions: The intact T = 13 IBDV (700 Å diameter) crystallizes in space group P21, with unit-cell parameters a = 854.0, b = 692.2, c = 792.4 Å (Coulibaly et al., 2005 ▶). Its cryo-TEM reconstruction at about 20 Å resolution was obtained with the RIco program based on micrographs produced by Jean Lepault. The crystal structure was solved by MR, but instead of the EM map we used the pseudo-atomic model resulting from the fit of the VP2 trimers into the EM map. The result of this fit is shown in Fig. 4 ▶; the correlation coefficient of this fit was 91.0% when using Fourier coefficients within the 400–35 Å resolution range. The virion capsid contains 260 VP2 trimers, of which only four and a third belong to the icosahedral asymmetric unit.


Combining X-ray and electron-microscopy data to solve crystal structures.

Navaza J - Acta Crystallogr. D Biol. Crystallogr. (2007)

Fit of the VP2 trimers into the cryo-TEM reconstruction of the T = 13 viral particle.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC2394810&req=5

fig4: Fit of the VP2 trimers into the cryo-TEM reconstruction of the T = 13 viral particle.
Mentions: The intact T = 13 IBDV (700 Å diameter) crystallizes in space group P21, with unit-cell parameters a = 854.0, b = 692.2, c = 792.4 Å (Coulibaly et al., 2005 ▶). Its cryo-TEM reconstruction at about 20 Å resolution was obtained with the RIco program based on micrographs produced by Jean Lepault. The crystal structure was solved by MR, but instead of the EM map we used the pseudo-atomic model resulting from the fit of the VP2 trimers into the EM map. The result of this fit is shown in Fig. 4 ▶; the correlation coefficient of this fit was 91.0% when using Fourier coefficients within the 400–35 Å resolution range. The virion capsid contains 260 VP2 trimers, of which only four and a third belong to the icosahedral asymmetric unit.

Bottom Line: Low-resolution electron-microscopy reconstructions can be used as search models in molecular replacement or may be combined with existing monomeric structures in order to produce multimeric models suitable for molecular replacement.The technique is described in the case of viral and subviral particles as well as in the case of oligomeric proteins.

View Article: PubMed Central - HTML - PubMed

Affiliation: Laboratoire de Microscopie Electronique Structurale, Institut de Biologie Structurale Jean-Pierre Ebel, 41 Rue Jules Horowitz, F-38027 Grenoble, France. jorge.navaza@ibs.fr

ABSTRACT
Low-resolution electron-microscopy reconstructions can be used as search models in molecular replacement or may be combined with existing monomeric structures in order to produce multimeric models suitable for molecular replacement. The technique is described in the case of viral and subviral particles as well as in the case of oligomeric proteins.

Show MeSH