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Acero, E.H., Ribitsch, D., Steinkellner, G., Gruber, K., Greimel, K., Eiteljoerg, I., Trotscha, E., Wei, R., Zimmermann, W., Zinee, M., Cavco-Paulo, A., Freddi, G., Schwab, H. and Guebitz, G. (2011) Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from Thermobifida. Macromolecules, 44, 4632-4640.
https://doi.org/10.1021/ma200949p

has been cited by the following article:

• TITLE: Expression, Purification and Crystallization of Thermostable Mutant of Cutinase Est1 from Thermobifida alba

  AUTHORS: Kengo Kitadokoro, Shingo Matsui, Ryouhei Osokoshi, Kensuke Nakata, Shigeki Kamitani

  KEYWORDS: Cutinase, Themobifida alba, Plastic Degrading Esterase, Crystallization, High Resolution Crystallographic Data

  JOURNAL NAME: Advances in Bioscience and Biotechnology, Vol.9 No.5, May 30, 2018

  ABSTRACT: A double mutantEst1, which is a plastic degrading cutinase-type esterase in Thermobifida alba, has been over-expressed in Escherichia coli. The recombinant protein was purified by a two-step protocol involving immobilized metal affinity chromatography and cation-exchange chromatography, yielding 120 mg of protein per liter of bacterial culture. Crystals have been obtained by using the sitting-drop vapor-diffusion technique. Native diffraction data to 1.37 Å resolution were obtained at the BL44XU beam line of SPring-8 from a flash-frozen crystal at 100 K. The crystals belong to space group C2, with unit-cell parameters a = 127.2 Å, b = 42.1 Å, c = 63.2 Å, β = 114.7°, likely containing one Est1 double mutant (296 residues) per asymmetric unit.