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 A 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 P2(1), with unit-cell parameters a = 31.5, b = 77.2, c = 38.5 A, beta = 107.4 degrees, and are likely to contain two extracellular domains (2 x 99 residues) per asymmetric unit.
Kitadokoro
K
K
Department of Physics--INFM and Advanced Biotechnology Center, University of Genoa, Via Dodecaneso 33, I-16146 Genova, Italy.
Galli
G
G
Petracca
R
R
Falugi
F
F
Grandi
G
G
Bolognesi
M
M
D015703:Antigens, CD / Q000737:chemistry* / Q000502:physiology; D001483:Base Sequence; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D016174:Hepacivirus / Q000502:physiology*; D006801:Humans; D008565:Membrane Proteins; D011991:Receptors, Virus / Q000737:chemistry* / Q000502:physiology; D011994:Recombinant Proteins / Q000737:chemistry; D060225:Tetraspanin 28
D015703:Antigens, CD; C554798:CD81 protein, human; D017931:DNA Primers; D008565:Membrane Proteins; D011991:Receptors, Virus; D011994:Recombinant Proteins; D060225:Tetraspanin 28