Cloning, purification, crystallization and preliminary crystallographic analysis of a penicillin-binding protein homologue from Pyrococcus abyssi
- Laboratoire de Recherche Moléculaire sur les Antibiotiques, INSERM U655, Université Pierre et Marie Curie (Paris 6), CHU Pitié-Salpêtrière, Paris (France)
- Laboratoire de Recherche Moléculaire sur les Antibiotiques, INSERM U655, Institut des Cordeliers, Paris (France)
The crystallization of a hypothetical penicillin-binding protein from the archaeon P. abyssi in space group C2 by hanging-drop vapour diffusion is reported. The genome of the hyperthermophilic archaeon Pyrococcus abyssi contains a gene (pab0087) encoding a penicillin-binding protein (PBP) homologue. This sequence consists of 447 residues and shows significant sequence similarity to low-molecular-weight PBPs and class C β-lactamases. The Pab0087 protein was overexpressed, purified and crystallized. Diffraction data from two different crystal forms were collected to 2.7 and 2.0 Å resolution. Both crystals belong to space group C2, with unit-cell parameters a = 160.59, b = 135.74, c = 113.02 Å, β = 117.36° and a = 166.97, b = 131.25, c = 189.39 Å, β = 113.81°, respectively. The asymmetric unit contains four and eight molecules, respectively, with fourfold non-crystallographic symmetry.
- OSTI ID:
- 22356184
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 11; Other Information: PMCID: PMC1978136; PMID: 16511220; PUBLISHER-ID: fw5050; OAI: oai:pubmedcentral.nih.gov:1978136; 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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