Haloalkane dehalogenase DmxA from Marinobacter sp. ELB17 possessing a unique catalytic residue

Deciphering the Structural Basis of High Thermostability of Dehalogenase from Psychrophilic BacteriumMarinobactersp. ELB17.

0.2M ammonium acetate, 30%(w/v) PEG 4000 and 0.1M sodium citrate tribasic dihydrate, additionally added sarcosine

Ministry of Education, Youth and Sports of the Czech Republic

U VALUES : WITH TLS ADDED HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS

hydrolase, thermostable enzyme, disulfide bridge, unique catalytic residue