MersV1, France, Analysis, bibRecord, 000299

Engineering of diffraction-quality crystals of the NF-κB P52 homodimer:DNA complex

Identifieur interne : 000299 ( France/Analysis ); précédent : 000298; suivant : 000300

Engineering of diffraction-quality crystals of the NF-κB P52 homodimer:DNA complex

Auteurs : Patrick Cramer [France] ; Christoph W. Müller [France]

Source :

FEBS Letters [ 0014-5793 ] ; 1997.

RBID : ISTEX:6D35CF52842B1624C667C120CD9D79B29FFCC606

English descriptors

Teeft :
- Amino, Amino acid position, Amino acid residues, Anisotropic diffraction, Asymmetric unit, Binding site, Complete dataset, Crystal form, Crystal forms, Crystallization, Crystallization screens, Data collection, Demineralized water, Different crystals, Diffracting form, Duplex, Dynamic light, Electrophoretic mobility shift assay, Final concentration, Flow rate, Forms table, Fplc system, General rules, Homology region, Linear gradient, Molecular weights, Nuclear localization signal, Peak fractions, Precipitant, Precipitant solution, Protein concentration, Protein engineering, Protein variant, Radiation damage, Reservoir solution, Room temperature, Solvent content, Space group, Synchrotron radiation, Third direction, Unit cell axis, Unit cell dimensions, Weak diffraction.

Abstract

Abstract: The eukaryotic transcription factors NF-κB P50 and NF-κB P52 are closely related members of the Rel family. Growth of diffraction-quality NF-κB P52:DNA co-crystals crucially depended on (a) extensive screens for the DNA fragment of optimal length and (b) engineering of the protein based on the two known NF-κB P50:DNA co-crystal structures [Müller et al. (1995) Nature 373, 311–317; Ghosh et al. (1995) Nature 373, 303–310]; namely, deletion of 12 C-terminal amino acid residues. These residues are part of the Rel homology region and comprise the nuclear localization signal. The approach might be of general use for the crystallization of other Rel protein:DNA complexes and in our case yielded co-crystals which diffract beyond 2.0 Å resolution. © 1997 Federation of European Biochemical Societies.

Url:

https://api.istex.fr/ark:/67375/6H6-211XRXPZ-J/fulltext.pdf

DOI: 10.1016/S0014-5793(97)00217-2

Affiliations:

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ISTEX:6D35CF52842B1624C667C120CD9D79B29FFCC606

Le document en format XML

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<front><div type="abstract" xml:lang="en">Abstract: The eukaryotic transcription factors NF-κB P50 and NF-κB P52 are closely related members of the Rel family. Growth of diffraction-quality NF-κB P52:DNA co-crystals crucially depended on (a) extensive screens for the DNA fragment of optimal length and (b) engineering of the protein based on the two known NF-κB P50:DNA co-crystal structures [Müller et al. (1995) Nature 373, 311–317; Ghosh et al. (1995) Nature 373, 303–310]; namely, deletion of 12 C-terminal amino acid residues. These residues are part of the Rel homology region and comprise the nuclear localization signal. The approach might be of general use for the crystallization of other Rel protein:DNA complexes and in our case yielded co-crystals which diffract beyond 2.0 Å resolution. © 1997 Federation of European Biochemical Societies.</div>
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Engineering of diffraction-quality crystals of the NF-κB P52 homodimer:DNA complex

Engineering of diffraction-quality crystals of the NF-κB P52 homodimer:DNA complex

Source :

English descriptors

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

Pour mettre un lien sur cette page dans le réseau Wicri