ISSN:
1399-0047
Source:
Crystallography Journals Online : IUCR Backfile Archive 1948-2001
Topics:
Chemistry and Pharmacology
,
Geosciences
,
Physics
Notes:
We have crystallized and performed preliminary X-ray characterization of the complex between the DNAase domain of the E9 colicin and its cognate immunity protein Im9. The dissociation constant for this complex, Kd = 1 × 10−16 M, reveals it to be one of the highest affinity protein–protein interactions known. Single crystals of the 1:1 complex were grown from microseeding experiments using PEG 4K as precipitant. The space group is P212121 with one molecule of complex in the asymmetric unit, and crystals contain approximately 43% solvent. These crystals are inherently non-isomorphous and so selenomethionine-derivatized protein has been prepared and crystals grown for MAD phasing experiments.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1107/S0108444998002590