Published March 12, 2005 | Version v1
Journal article

Crystallization and preliminary X-ray analysis of immunophilin-like FKBP42 from Arabidopsis thaliana

  • 1. Institut für Biologische Informationsverarbeitung (IBI-2, Biologische Strukturforschung), Forschungszentrum Jülich GmbH, D-52425 Jülich (Germany)
  • 2. Max-Planck-Forschungsstelle für Enzymologie der Proteinfaltung, D-06120 Halle (Germany)
  • 3. Purdue University, Department of Horticulture and Landscape Architecture, West Lafayette, IN 47907 (United States)
  • 4. Universität Tübingen, ZMBP, D-72076 Tübingen (Germany)

Description

The crystallization of FKBP42, a multi-domain member of the FK506-binding protein family, from the plant A. thaliana is reported. Two fragments of FKBP42 from Arabidopsis thaliana covering differing lengths of the molecule have been expressed, purified and crystallized. For each construct, crystals belonging to two different space groups were obtained and subjected to preliminary X-ray analysis

Availability note (English)

Available from http://dx.doi.org/10.1107/S1744309105006342; Available from http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1952426

Additional details

Publishing Information

Journal Title
Acta Crystallographica. Section F
Journal Volume
61
Journal Issue
Pt 4
Journal Page Range
p. 363-365
ISSN
1744-3091
CODEN
ACSFCL

INIS

Country of Publication
United Kingdom
Country of Input or Organization
International Atomic Energy Agency (IAEA)
INIS RN
46061289
Subject category
S75: CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY;
Descriptors DEI
COVERINGS; CRYSTALLIZATION; CRYSTALS; LENGTH; MOLECULES; SPACE GROUPS
Descriptors DEC
DIMENSIONS; PHASE TRANSFORMATIONS; SYMMETRY GROUPS

Optional Information

Copyright
Copyright (c) International Union of Crystallography 2005
Notes
PMCID: PMC1952426; PMID: 16511041; PUBLISHER-ID: za5091; OAI: oai:pubmedcentral.nih.gov:1952426