Open AccessCrystallization of the C‐terminal domain of the fibre protein from snake adenovirus 1, an atadenovirus
Author(s) -
Singh Abhimanyu K.,
MenéndezConejero Rosa,
San Martín Carmen,
van Raaij Mark J.
Publication year - 2013
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309113029308
Subject(s) - crystallization , resolution (logic) , protein crystallization , domain (mathematical analysis) , leucine , mutagenesis , adenoviridae , mastadenovirus , biology , biophysics , recombinant dna , chemistry , crystallography , biochemistry , amino acid , mutation , mathematical analysis , mathematics , organic chemistry , artificial intelligence , computer science , gene
Adenovirus fibre proteins play an important role in determining viral tropism. The C‐terminal domain of the fibre protein from snake adenovirus type 1, a member of the Atadenovirus genus, has been expressed, purified and crystallized. Crystals were obtained belonging to space groups P 2 1 2 1 2 1 (two different forms), I 2 1 3 and F 23. The best of these diffracted synchrotron radiation to a resolution of 1.4 Å. As the protein lacks methionines or cysteines, site‐directed mutagenesis was performed to change two leucine residues to methionines. Crystals of selenomethionine‐derivatized crystals of the I 2 1 3 form were also obtained and a multi‐wavelength anomalous dispersion data set was collected.