Crystal Structure of Rat Synapsin I C Domain Complexed to Ca.ATP (Form 1)

Tetramerization and ATP binding by a protein comprising the A, B, and C domains of rat synapsin I.

Synapsin I is structurally similar to ATP-utilizing enzymes

Horizontally bent Si(111), with monochromatic mirrors of Rh-coated Si

PEGMME 5K, Tris, NaCl, Ca.ATP, EDTA, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 299K

Bovine Synapsin I C domain complexed to Ca.ATP-gamma-S

Although the A, B, and C domains of rat synapsin I were included in crystallization, only the C domain was observed. Some residues have side chains that are set to occupancies of 0.00 due to disorder.
PDB entry 1AUX, Ca and ATP-gamma-S removed

The second half of the (presumably) biological tetramer is generated by the twofold axis: -y + 1, -x + 1, -z + 1/6

ATP binding, ATP grasp, calcium (II) ion, MEMBRANE PROTEIN