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Title: Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase

Abstract

Human ADP-ribosylhydrolase 3 (ARH3), which has been identified as an ARH by a sequence-similarity search and which cleaves the glycosidic bond of ADP-ribose attached to a protein, has been cloned, expressed, purified and crystallized in two different space groups. ADP-ribosylhydrolases catalyze the release of ADP-ribose from ADP-ribosylated proteins via hydrolysis of the glycosidic bond between ADP-ribose and a specific amino-acid residue in a target protein. Human ADP-ribosylhydrolase 3, consisting of 347 amino-acid residues, has been cloned and heterologously expressed in Escherichia coli, purified and crystallized in two different space groups. Preliminary X-ray diffraction studies yielded excellent diffraction data to a resolution of 1.6 Å.

Authors:
;  [1]; ; ;  [2];  [3]
  1. Institut für Immunologie, Universitätsklinikum Eppendorf, D-20246 Hamburg (Germany)
  2. EMBL Outstation Hamburg, c/o DESY Notkestrasse 85, D-22603 Hamburg (Germany)
  3. (Germany)
Publication Date:
OSTI Identifier:
22356281
Resource Type:
Journal Article
Resource Relation:
Journal Name: Acta Crystallographica. Section F; Journal Volume: 62; Journal Issue: Pt 3; Other Information: PMCID: PMC2197168; PMID: 16511307; PUBLISHER-ID: bw5130; OAI: oai:pubmedcentral.nih.gov:2197168; 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; ESCHERICHIA COLI; PROTEINS; RESOLUTION; SPACE GROUPS; X-RAY DIFFRACTION

Citation Formats

Kernstock, Stefan, Koch-Nolte, Friedrich, Mueller-Dieckmann, Jochen, Weiss, Manfred S., Mueller-Dieckmann, Christoph, E-mail: dieckman@embl-hamburg.de, and Institut für Immunologie, Universitätsklinikum Eppendorf, D-20246 Hamburg. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase. United Kingdom: N. p., 2006. Web. doi:10.1107/S1744309106003435.
Kernstock, Stefan, Koch-Nolte, Friedrich, Mueller-Dieckmann, Jochen, Weiss, Manfred S., Mueller-Dieckmann, Christoph, E-mail: dieckman@embl-hamburg.de, & Institut für Immunologie, Universitätsklinikum Eppendorf, D-20246 Hamburg. Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase. United Kingdom. doi:10.1107/S1744309106003435.
Kernstock, Stefan, Koch-Nolte, Friedrich, Mueller-Dieckmann, Jochen, Weiss, Manfred S., Mueller-Dieckmann, Christoph, E-mail: dieckman@embl-hamburg.de, and Institut für Immunologie, Universitätsklinikum Eppendorf, D-20246 Hamburg. Wed . "Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase". United Kingdom. doi:10.1107/S1744309106003435.
@article{osti_22356281,
title = {Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of human ARH3, the first eukaryotic protein-ADP-ribosylhydrolase},
author = {Kernstock, Stefan and Koch-Nolte, Friedrich and Mueller-Dieckmann, Jochen and Weiss, Manfred S. and Mueller-Dieckmann, Christoph, E-mail: dieckman@embl-hamburg.de and Institut für Immunologie, Universitätsklinikum Eppendorf, D-20246 Hamburg},
abstractNote = {Human ADP-ribosylhydrolase 3 (ARH3), which has been identified as an ARH by a sequence-similarity search and which cleaves the glycosidic bond of ADP-ribose attached to a protein, has been cloned, expressed, purified and crystallized in two different space groups. ADP-ribosylhydrolases catalyze the release of ADP-ribose from ADP-ribosylated proteins via hydrolysis of the glycosidic bond between ADP-ribose and a specific amino-acid residue in a target protein. Human ADP-ribosylhydrolase 3, consisting of 347 amino-acid residues, has been cloned and heterologously expressed in Escherichia coli, purified and crystallized in two different space groups. Preliminary X-ray diffraction studies yielded excellent diffraction data to a resolution of 1.6 Å.},
doi = {10.1107/S1744309106003435},
journal = {Acta Crystallographica. Section F},
number = Pt 3,
volume = 62,
place = {United Kingdom},
year = {Wed Mar 01 00:00:00 EST 2006},
month = {Wed Mar 01 00:00:00 EST 2006}
}
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