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

نویسندگان

  • Yury A Kislitsyn
  • Valeriya R Samygina
  • Igor A Dvortsov
  • Nataliya A Lunina
  • Inna P Kuranova
  • Galina A Velikodvorskaya
چکیده

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.

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عنوان ژورنال:
  • Acta crystallographica. Section F, Structural biology communications

دوره 71 Pt 2  شماره 

صفحات  -

تاریخ انتشار 2015