Characterization of crystals of the Hjc resolvase from Archaeoglobus fulgidus grown in gel by counter-diffusion
- European Molecular Biology Laboratory, Structural and Computational Biology Programme, Meyerhofstrasse 1, 69117 Heidelberg (Germany)
The Holliday junction-cutting enzyme Hjc from A. fulgidus was crystallized by the counter-diffusion method in agarose gel and complete data were collected at 2.7 Å resolution using synchrotron radiation. Holliday junction-resolving enzymes are ubiquitous proteins that play a key role in DNA repair and reorganization by homologous recombination. The Holliday junction-cutting enzyme (Hjc) from the archaeon Archaeoglobus fulgidus is a member of this group. The first Hjc crystals were obtained by conventional sparse-matrix screening. They exhibited an unusually elongated unit cell and their X-ray characterization required special care to avoid spot overlaps along the c* axis. The use of an arc appended to the goniometric head allowed proper orientatation of plate-like crystals grown in agarose gel by counter-diffusion. Thus, complete diffraction data were collected at 2.7 Å resolution using synchrotron radiation. They belong to space group P3{sub 1}21 or P3{sub 2}21, with unit-cell parameters a = b = 37.4, c = 271.8 Å.
- OSTI ID:
- 22356133
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 7; Other Information: PMCID: PMC1952446; PMID: 16511128; PUBLISHER-ID: za5109; OAI: oai:pubmedcentral.nih.gov:1952446; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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