Crystallization and preliminary X-ray diffraction studies of the family 54 carbohydrate-binding module from laminarinase (?-1,3-glucanase) Lic16A of Clostridium thermocellum.

ABSTRACT: The crystallization and preliminary X-ray diffraction analysis of the carbohydrate-binding module (CBM) from laminarinase Lic16A of the hyperthermophilic anaerobic bacterium Clostridium thermocellum (ctCBM54) are reported. Recombinant ctCBM54 was prepared using an Escherichia coli/pQE30 overexpression system and was crystallized by the hanging-drop vapour-diffusion method. X-ray diffraction data were collected to 2.1 Å resolution using synchrotron radiation. The crystals belonged to space group P6322, with unit-cell parameters a = b = 130.15, c = 131.05 Å. The three-dimensional structure of ctCBM54 will provide valuable information about the structure-function relation of the laminarinase Lic16A and will allow the exploitation of this binding module in biotechnological applications.

SUBMITTER: Kislitsyn YA 

PROVIDER: S-EPMC4321479 | biostudies-literature | 2015 Feb

REPOSITORIES: biostudies-literature