New avenues for cancer research from protein nanocrystallography

Description

As a result of cooperation between the Nanoworld Institute and the European Synchrotron Radiation Facility in Grenoble, after the initial discovery of the atomic structure of human kinase CK2alpha we have introduced new further developments in protein nanocrystallography, appearing to have profound potential impact in cancer research. First of all, new details in protein crystal topography appear evident in conjuction also with AFM experimentations. The obtained images point to the existence of clear domains in the crystal 3D organization, quite pronounced and different in size and number between the classical protein crystals and the crystals grown by LB (Langmuir-Blodgett) protein nanotemplate. This result is furthermore in perfect accordance with that obtained by laser cutting of the corresponding protein crystals down to the nanosize and along the crystal domains. X-ray diffraction with highly focused synchrotron radiation down to 500 nm diameter strikingly provides unique and detailed atomic structure information in protein microcrystals down to the submicron size in several model systems, opening new avenues in protein crystallography. With radiation damage being the most critical issue for protein structure determination under the intense synchrotron radiation, LB crystals were indeed confirmed as the most stable to radiation damage in a wide range of model systems. Crystals grown by nanotemplate still diffract at good resolution even after several steps of X-ray "burning", while the classic crystals decay very quickly at the same exposure. Finally due to this encouraging result, the LB method has also been successfully adapted to the EMBL advanced robotics system for protein crystallography and to the study of yet unsolved protein systems such as ribosomal proteins.

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