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. A1 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 P21 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.
CITATION STYLE
Mishima, Y., Momma, K., Hashimoto, W., Mikami, B., & Murata, K. (2001). Crystallization and preliminary X-ray analysis of AlgS, a bacterial ATP-binding cassette (ABC) protein specific to macromolecule import. Acta Crystallographica Section D: Biological Crystallography, 57(6), 884–885. https://doi.org/10.1107/S090744490100525X
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