Crystallization and Preliminary X-ray Diffraction Analysis of the Human Dimeric S-Lac Lectin (L-14-II)

The human recombinant S-Lac lectin, L-14-II, produced in an Escherichia coli expression system, has been co-crystallized in the presence of lactose by the hanging drop vapor diffusion method. The crystals grow in space group P2 12 12 1 with unit cell dimensions of a = 43·6 Å, b = 57·8 Å, c = 108·2 Å...

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Veröffentlicht in:Journal of molecular biology 1993-10, Vol.233 (3), p.553-555
Hauptverfasser: Lobsanov, Yuri D., Gitt, Michael A., Leffler, Hakon, Barondes, Samuel, Rini, James M.
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Sprache:eng
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Zusammenfassung:The human recombinant S-Lac lectin, L-14-II, produced in an Escherichia coli expression system, has been co-crystallized in the presence of lactose by the hanging drop vapor diffusion method. The crystals grow in space group P2 12 12 1 with unit cell dimensions of a = 43·6 Å, b = 57·8 Å, c = 108·2 Å, with a dimer in the asymmetric unit. On a conventional rotating anode the crystals diffract to at least 2·8 Å resolution.
ISSN:0022-2836
1089-8638
DOI:10.1006/jmbi.1993.1533