TY - JOUR
T1 - Crystallization and preliminary X-ray diffraction analysis of protein 14 from Sulfolobus islandicus filamentous virus (SIFV)
AU - Goulet, Adeline
AU - Spinelli, Silvia
AU - Campanacci, Valérie
AU - Porciero, Sophie
AU - Blangy, Stéphanie
AU - Garrett, Roger A
AU - van Tilbeurgh, Herman
AU - Leulliot, Nicolas
AU - Basta, Tamara
AU - Prangishvili, David
AU - Cambillau, Christian
N1 - Keywords: Cloning, Molecular; Crystallization; Lipothrixviridae; Sulfolobus; Viral Proteins; X-Ray Diffraction
PY - 2006
Y1 - 2006
N2 - A large-scale programme has been embarked upon aiming towards the structural determination of conserved proteins from viruses infecting hyperthermophilic archaea. Here, the crystallization of protein 14 from the archaeal virus SIFV is reported. This protein, which contains 111 residues (MW 13 465 Da), was cloned and expressed in Escherichia coli with an N-terminal His(6) tag and purified to homogeneity. The tag was subsequently cleaved and the protein was crystallized using PEG 1000 or PEG 4000 as a precipitant. Large crystals were obtained of the native and the selenomethionine-labelled protein using sitting drops of 100-300 nl. Crystals belong to space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 68.1, c = 132.4 A. Diffraction data were collected to a maximum acceptable resolution of 2.95 and 3.20 A for the SeMet-labelled and native protein, respectively.
AB - A large-scale programme has been embarked upon aiming towards the structural determination of conserved proteins from viruses infecting hyperthermophilic archaea. Here, the crystallization of protein 14 from the archaeal virus SIFV is reported. This protein, which contains 111 residues (MW 13 465 Da), was cloned and expressed in Escherichia coli with an N-terminal His(6) tag and purified to homogeneity. The tag was subsequently cleaved and the protein was crystallized using PEG 1000 or PEG 4000 as a precipitant. Large crystals were obtained of the native and the selenomethionine-labelled protein using sitting drops of 100-300 nl. Crystals belong to space group P6(2)22 or P6(4)22, with unit-cell parameters a = b = 68.1, c = 132.4 A. Diffraction data were collected to a maximum acceptable resolution of 2.95 and 3.20 A for the SeMet-labelled and native protein, respectively.
U2 - 10.1107/S1744309106029150
DO - 10.1107/S1744309106029150
M3 - Journal article
C2 - 16946470
SN - 2053-230X
VL - 62
SP - 884
EP - 886
JO - Acta Crystallographica Section F: Structural Biology Communications
JF - Acta Crystallographica Section F: Structural Biology Communications
IS - Pt 9
ER -