@article{3048384,
    title = "A triclinic crystal form of the lectin concanavalin A",
    author = "Kanellopoulos, PN and Tucker, PA and Pavlou, K and Agianian, B and and Hamodrakas, SJ",
    journal = "Journal of Structural Biology",
    year = "1996",
    volume = "117",
    number = "1",
    pages = "16-23",
    publisher = "ACADEMIC PRESS INC ELSEVIER SCIENCE",
    issn = "1047-8477, 1095-8657",
    doi = "10.1006/jsbi.1996.0065",
    abstract = "The molecular structure of a triclinic crystal form of concanavalin A
has been refined at 2.4 Angstrom resolution. The crystals have unit cell
dimensions a 78.8 Angstrom, b = 79.3 Angstrom, c = 133.3 Angstrom, alpha
= 97.1 degrees, beta = 90.2 degrees, and gamma = 97.5 degrees and
contain two tetramers per asymmetric unit each with approximate 222
symmetry. The final crystallographic R-factor is 0.205 and the
free-R-factor is 0.265 in the resolution range 6.0 to 2.4 Angstrom The
conformation of the tetramer is more similar to that found in
concanavalin A saccharide complexes than in the previously reported I222
crystal form of uncomplexed concanavalin A. A comparison of the
molecular packing between the two crystal forms shows a more open
arrangement with large solvent channels through the crystal. (C) 1996
Academic Press, Inc."
}