Crystallographic characterization of the membrane-binding domain of radixin

Citation
K. Hamada et al., Crystallographic characterization of the membrane-binding domain of radixin, ACT CRYST D, 56, 2000, pp. 922-923
Citations number
18
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
7
Pages
922 - 923
Database
ISI
SICI code
0907-4449(200007)56:<922:CCOTMD>2.0.ZU;2-P
Abstract
Radixin is a protein which cross-links plasma membranes and actin filaments and thus forms membrane-associated cytoskeleton. The radixin N-terminal do main, which is responsible for membrane association, has been purified and crystallized by vapour diffusion with polyethylene glycol 6000. The crystal s belong to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = b = 96.36, c = 133.16 Angstrom, and diffract to a resolution of 3.0 An gstrom.