Crystallization and preliminary crystallographic studies on the large extracellular domain of human CD81, a tetraspanin receptor for hepatitis C virus
The large extracellular domain of CD81, a member of the tetraspanin family and a receptor protein for hepatitis C virus envelope E2 glycoprotein, has been expressed, purified and subsequently crystallized using the sitting‐drop vapour‐diffusion technique. Native diffraction data to 1.6 Å resolution...
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Veröffentlicht in: | Acta crystallographica. Section D, Biological crystallography. Biological crystallography., 2001-01, Vol.57 (1), p.156-158 |
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Format: | Artikel |
Sprache: | eng |
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Zusammenfassung: | The large extracellular domain of CD81, a member of the tetraspanin family and a receptor protein for hepatitis C virus envelope E2 glycoprotein, has been expressed, purified and subsequently crystallized using the sitting‐drop vapour‐diffusion technique. Native diffraction data to 1.6 Å resolution were obtained at the ID14 beamline of the European Synchrotron Radiation Facility from a flash‐frozen crystal at 100 K. The crystals belong to space group P21, with unit‐cell parameters a = 31.5, b = 77.2, c = 38.5 Å, β = 107.4°, and are likely to contain two extracellular domains (2 × 99 residues) per asymmetric unit. |
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ISSN: | 1399-0047 0907-4449 1399-0047 |
DOI: | 10.1107/S0907444900015468 |