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Title: Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1

Abstract

Human RuvB-like protein RuvBL1 plays important roles in essential signaling pathways like c-Myc and Wnt, in transcription, and in DNA repair and apoptosis. Crystals of both native and a Se-Met derivative were obtained and characterized. SAD data leading to the structure solution at 2.2 Å were measured from the Se-Met crystals. RuvBL1, an evolutionary highly conserved protein related to the AAA{sup +} family of ATPases, has been crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystals are hexagonal and belong to space group P6, with unit-cell parameters a = b = 207.1, c = 60.7 Å and three molecules in the asymmetric unit.

Authors:
 [1];  [2];  [1];  [1];  [3]; ;  [1];  [4];  [5];  [6];  [5];  [1]
  1. ITQB - Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Apartado 127, 2781-901 Oeiras (Portugal)
  2. (Germany)
  3. (France)
  4. IBET - Instituto de Biologia Experimental e Tecnológica, Apartado 12, 2781-901 Oeiras (Portugal)
  5. Schering AG, Protein Chemistry/Enabling Technologies, 13342 Berlin (Germany)
  6. Schering AG, Cooperate Research Oncology, 13342 Berlin (Germany)
Publication Date:
OSTI Identifier:
22356240
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 1; Other Information: PMCID: PMC2150925; PMID: 16511264; PUBLISHER-ID: en5150; OAI: oai:pubmedcentral.nih.gov:2150925; Copyright (c) International Union of Crystallography 2006; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United Kingdom
Language:
English
Subject:
75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTALLIZATION; CRYSTALS; DIFFUSION; MATHEMATICAL SOLUTIONS; MOLECULES; PROTEINS; SOLUTIONS; SPACE GROUPS

Citation Formats

Gorynia, Sabine, Schering AG, Protein Chemistry/Enabling Technologies, 13342 Berlin, Matias, Pedro M., Gonçalves, Susana, ESRF, European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, BP 220, F-38043 Grenoble CEDEX, Coelho, Ricardo, Lopes, Gonçalo, Thomaz, Mónica, Huber, Martina, Haendler, Bernard, Donner, Peter, and Carrondo, Maria Arménia, E-mail: carrondo@itqb.unl.pt. Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309105041400.
Gorynia, Sabine, Schering AG, Protein Chemistry/Enabling Technologies, 13342 Berlin, Matias, Pedro M., Gonçalves, Susana, ESRF, European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, BP 220, F-38043 Grenoble CEDEX, Coelho, Ricardo, Lopes, Gonçalo, Thomaz, Mónica, Huber, Martina, Haendler, Bernard, Donner, Peter, & Carrondo, Maria Arménia, E-mail: carrondo@itqb.unl.pt. Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1. United Kingdom. doi:10.1107/S1744309105041400.
Gorynia, Sabine, Schering AG, Protein Chemistry/Enabling Technologies, 13342 Berlin, Matias, Pedro M., Gonçalves, Susana, ESRF, European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, BP 220, F-38043 Grenoble CEDEX, Coelho, Ricardo, Lopes, Gonçalo, Thomaz, Mónica, Huber, Martina, Haendler, Bernard, Donner, Peter, and Carrondo, Maria Arménia, E-mail: carrondo@itqb.unl.pt. Sun . "Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1". United Kingdom. doi:10.1107/S1744309105041400.
@article{osti_22356240,
title = {Expression, purification, crystallization and preliminary X-ray analysis of the human RuvB-like protein RuvBL1},
author = {Gorynia, Sabine and Schering AG, Protein Chemistry/Enabling Technologies, 13342 Berlin and Matias, Pedro M. and Gonçalves, Susana and ESRF, European Synchrotron Radiation Facility, 6 Rue Jules Horowitz, BP 220, F-38043 Grenoble CEDEX and Coelho, Ricardo and Lopes, Gonçalo and Thomaz, Mónica and Huber, Martina and Haendler, Bernard and Donner, Peter and Carrondo, Maria Arménia, E-mail: carrondo@itqb.unl.pt},
abstractNote = {Human RuvB-like protein RuvBL1 plays important roles in essential signaling pathways like c-Myc and Wnt, in transcription, and in DNA repair and apoptosis. Crystals of both native and a Se-Met derivative were obtained and characterized. SAD data leading to the structure solution at 2.2 Å were measured from the Se-Met crystals. RuvBL1, an evolutionary highly conserved protein related to the AAA{sup +} family of ATPases, has been crystallized using the hanging-drop vapour-diffusion method at 293 K. The crystals are hexagonal and belong to space group P6, with unit-cell parameters a = b = 207.1, c = 60.7 Å and three molecules in the asymmetric unit.},
doi = {10.1107/S1744309105041400},
journal = {Acta Crystallographica. Section F},
number = Pt 1,
volume = 62,
place = {United Kingdom},
year = {Sun Jan 01 00:00:00 EST 2006},
month = {Sun Jan 01 00:00:00 EST 2006}
}
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