STRUCTURE OF THE C DOMAIN OF SYNAPSIN IA FROM BOVINE BRAIN WITH CALCIUM ATP-GAMMA-S BOUND

PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER
ATP-GAMMA-S; ADENOSINE 5'-(3-THIOTRIPHOSPHATE); ADENOSINE 5'-(GAMMA-THIOTRIPHOSPHATE); ADENOSINE-5'-DIPHOSPHATE MONOTHIOPHOSPHATE

Synapsin I is structurally similar to ATP-utilizing enzymes.

Identification, Expression, and Crystallization of the Protease-Resistant Conserved Domain of Synapsin I

Synapsins: Mosaics of Shared and Individual Domains in a Family of Synaptic Vesicle Phosphoproteins

PROTEIN WAS CRYSTALLIZED FROM 5 % PEG 4000, 100 MM HEPES, PH 7.25, THEN DIRECTLY TRANSFERRED TO 30 % PEG 4000, 50 MM HEPES, PH 7.5, 50 MM NACL. AFTER 12 H, CRYSTALS WERE TRANSFERRED TO 30 % PEG, 75 MM HEPES, PH 7.5, 75 MM NACL, 2.5 MM CACL2, 2.5 MM ATP-GAMMA-S FOR 23 H.

ONE CALCIUM ION AND ONE MOLECULE OF ADENOSINE DIPHOSPHATE MONOTHIOPHOSPHATE (ATP-GAMMA-S) ARE BOUND PER MONOMER.

SYNAPSE, PHOSPHORYLATION, SYNAPSIN IA C-DOMAIN, ATP-BINDING, TRANSFERASE