Structure of the ARTT motif E214N mutant C3bot1 Exoenzyme (Free state, crystal form III)

Structural Basis for the Nad-Hydrolysis Mechanism and the Artt-Loop Plasticity of C3 Exoenzymes.

Nad Binding Induces Conformational Changes in Rho Adp-Ribosylating Clostridium Botulinum C3 Exoenzyme.

22.5% PEG 3350 W/W, 100 MM LI2SO4, 100 MM SODIUM CITRATE PH 3.0,3-10% MPEG 550 V/V

THE CRYSTAL STRUCTURE OF EXOENZYME C3 FROM CLOSTRIDIUM BOTULINUM

STRUCTURE OF THE CLOSTRIDIUM BOTULINUM C3 EXOENZYME (L177C MUTANT)

C3 EXOENZYME FROM CLOSTRIDIUM BOTULINUM, TETRAGONAL FORM

STRUCTURE OF THE CLOSTRIDIUM BOTULINUM C3 EXOENZYME (WILD-TYPE) IN COMPLEX WITH NAD

STRUCTURE OF THE WILD-TYPE C3BOT1 EXOENZYME (NICOTINAMIDE-BOUND STATE, CRYSTAL FORM I)

STRUCTURE OF THE ARTT MOTIF Q212A MUTANT C3BOT1 EXOENZYME (FREE STATE, CRYSTAL FORM II)

STRUCTURE OF THE ARTT MOTIF Q212A MUTANT C3BOT1 EXOENZYME (NAD-BOUND STATE, CRYSTAL FORM I)

STRUCTURE OF THE ARTT MOTIF Q212A MUTANT C3BOT1 EXOENZYME (FREE STATE, CRYSTAL FORM I)

STRUCTURE OF THE ARTT MOTIF E214N MUTANT C3BOT1 EXOENZYME (NAD-BOUND STATE, CRYSTAL FORM III)

STRUCTURE OF THE PN LOOP Q182A MUTANT C3BOT1 EXOENZYME (FREE STATE, CRYSTAL FORM I)

STRUCTURE OF THE PN LOOP Q182A MUTANT C3BOT1 EXOENZYME (NAD-BOUND STATE, CRYSTAL FORM I)

ENGINEERED RESIDUE IN CHAIN E, GLU 214 TO ASN ENGINEERED RESIDUE IN CHAIN F, GLU 214 TO ASN ENGINEERED RESIDUE IN CHAIN G, GLU 214 TO ASN

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS.

MONO-ADP-RIBOSYLTRANSFERASE C3 (E.C.2.4.2.-)

C3 EXOENZYME, ARTT MOTIF, BACTERIAL TOXINS, TRANSFERASE, GLYCOSYLTRANSFERASE