Abstract
The N-terminal portion (amino acids 1303-1367) of the type 1 ryanodine receptor D2 region is thought to be critical for excitation-contraction coupling in skeletal muscle. A segment of the D2 region (amino acids 1317-1355) was expressed as a glutathione S-transferase fusion protein (GST-D2) and then crystallized at room temperature using ammonium sulfate as precipitant. Using a newly developed cryo-soaking method, complete native data sets were measured to a resolution of 2.2 A using synchrotron radiation. The crystal was found to be hexagonal, belonging to space group P6(3)22, with unit-cell parameters a = b = 116.1, c = 77.9 A.
Publication types
-
Research Support, Non-U.S. Gov't
MeSH terms
-
Animals
-
Crystallization
-
Electrophoresis, Polyacrylamide Gel
-
Glutathione Transferase / biosynthesis
-
Glutathione Transferase / genetics
-
Muscle Fibers, Fast-Twitch / chemistry*
-
Muscle, Skeletal / chemistry*
-
Peptide Fragments / biosynthesis
-
Peptide Fragments / chemistry*
-
Peptide Fragments / genetics
-
Rabbits
-
Recombinant Fusion Proteins / biosynthesis
-
Recombinant Fusion Proteins / genetics
-
Ryanodine Receptor Calcium Release Channel / biosynthesis
-
Ryanodine Receptor Calcium Release Channel / chemistry*
-
Ryanodine Receptor Calcium Release Channel / genetics
-
Sodium Dodecyl Sulfate
Substances
-
Peptide Fragments
-
Recombinant Fusion Proteins
-
Ryanodine Receptor Calcium Release Channel
-
Sodium Dodecyl Sulfate
-
Glutathione Transferase