The molecular-replacement solution of an intermediate-sized helical polypeptide, antiamoebin I.
The successful use of molecular-replacement methods for the solution of the intermediate-sized helical polypeptide antiamoebin I required the careful consideration of a number of parameters and exhibited some unusual characteristics when compared with molecular-replacement solutions of globular proteins. High-resolution data were required owing to several features, including the comma-like shape of the molecule (which results in a pseudo-symmetric structure at low resolution), the relative uniformity of the structure in the direction along the helix axis and the small differences between the two independent molecules in the P1 asymmetric unit. Other parameters which were important for the solution of this relatively low solvent content closely packed cell included the radius of integration, the use of normalized structure factors and especially the choice of starting model.
Snook
C F
CF
Department of Crystallography, Birkbeck College, University of London, London WC1E 7HX, England. ubcg91c@ccs.bbk.ac.uk
Wallace
B A
BA
D000595:Amino Acid Sequence; D000900:Anti-Bacterial Agents / Q000737:chemistry*; D018360:Crystallography, X-Ray / Q000379:methods; D008958:Models, Molecular; D008969:Molecular Sequence Data; D054848:Peptaibols; D010455:Peptides; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D012996:Solutions
D000900:Anti-Bacterial Agents; D054848:Peptaibols; D010455:Peptides; D012996:Solutions; C006596:antiamoebin