Crystal structure of apo-Aspartoacylase from human brain

Examination of the Mechanism of Human Brain Aspartoacylase through the Binding of an Intermediate Analogue.

Kirkpatrick-Baez pair of focusing bimorph mirrors

MTSCHIAEEHIQKVAIFGGTHGNELTGVFLVKHWLENGAEIQRTGLEVKPFITNPRAVKKCTRYIDCDLNRIFDLENLGK
KMSEDLPYEVRRAQEINHLFGPKDSEDSYDIIFDLHNTTSNMGCTLILEDSRNNFLIQMFHYIKTSLAPLPCYVYLIEHP
SLKYATTRSIAKYPVGIEVGPQPQGVLRADILDQMRKMIKHALDFIHHFNEGKEFPPCAIEVYKIIEKVDYPRDENGEIA
AIIHPNLQDQDWKPLHPGDPMFLTLDGKTIPLGGDCTVYPVFVNEAAYYEKKEAFAKTTKLTLNAKSIRCCLH

Protein concentration 8-10 mg/ml, 0.05 M Sodium citrate pH 6.0, 0.3 M K2HPO4, 19% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K

Complex Crystal Structure of human Aspartoacylase with Intermediate Analog (N-phosphonomethyl-L-aspartate)

HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

The second part of the biological assembly is generated by the two fold axis: -x, -y, z.

CANAVAN DISEASE, N-ACETYL-L-ASPARTATE, ZINC-DEPENDENT HYDROLASE, ASPARTOACYLASE FAMILY, AMINOACYLASE-2, ACY2, ASPA, N-phosphonomethyl-L-aspartate, HYDROLASE