Crystallization and preliminary characterization of crystals of the C-terminal half fragment of tropomodulin.
Tropomodulin (40 kDa) stabilizes the actin-tropomyosin filament by capping the P end (slow-growing end). The C-terminal half (C20, 20 kDa), an independently folded domain that is believed to be responsible for the P-end capping, has been crystallized. Crystals grew in the presence of Zn(2+) as the solution pH was increased from 3 towards the pI of the protein. The crystals belong to the trigonal space group R3. They have unit-cell parameters a = b = 69.6, c = 101.3 A (mean values, with a estimated standard deviation of 0.009 A) and diffract to 1.9 A resolution when the frozen crystals were measured at 120 K on a rotating-anode X-ray source at 120 K.
Krieger
I
I
RIKEN Harima Institute at Spring-8, Laboratory for Structural Biochemistry, Kouto, Mikazuki, Sayo, Hyogo 679-5148, Japan.
Kostyukova
A S
AS
Maéda
Y
Y
D002352:Carrier Proteins / Q000737:chemistry*; D003460:Crystallization; D018360:Crystallography, X-Ray; D008840:Microfilament Proteins; D010446:Peptide Fragments / Q000737:chemistry; D011487:Protein Conformation; D051348:Tropomodulin
D002352:Carrier Proteins; D008840:Microfilament Proteins; D010446:Peptide Fragments; D051348:Tropomodulin