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Crystallization and preliminary X-ray analysis of AlgS, a bacterial ATP-binding cassette (ABC) protein specific to macromolecule import.
- Source :
- Acta Crystallographica: Section D (Wiley-Blackwell); Jun2001, Vol. 57 Issue 6, p884-885, 2p
- Publication Year :
- 2001
-
Abstract
- Sphingomonas sp. A1 possesses a macromolecule (alginate; average molecular size 25 700 Da) uptake system mediated by a novel pit-dependent ABC transporter. In this system, AlgS (363 amino-acid residues; 40 kDa) functions as an ATPase and provides energy for the translocation of high molecular-weight alginate across the cytoplasmic membrane. Hexahistidine-tagged AlgS of Sphingomonas sp. Al was overexpressed in Escherichia coli and crystallized by means of the hanging-drop vapour-diffusion method with ammonium dihydrogen monophosphate as the precipitant. Preliminary X-ray analysis of the resultant crystals was performed; they belonged to the monoclinic space group P2<subscript>1</subscript> and had unit-cell parameters a = 57.4, b = 92.7, c = 65.8 Å, β = 102.3°. X-ray diffraction data to 3.2 Å have been collected from the native crystal. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09074449
- Volume :
- 57
- Issue :
- 6
- Database :
- Complementary Index
- Journal :
- Acta Crystallographica: Section D (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 15000650
- Full Text :
- https://doi.org/10.1107/S090744490100525X