LANGMUIR-BLODGETT NANOTEMPLATE CRYSTALLIZATION COMBINED TO LASER-MICROFRAGMENTATION UNIQUELY CHARACTERIZE PROTEINS CRYSTALS BY SYNCHROTRON MICRODIFFRACTION

Abstract

Laser-induced microfragmentation of LB nanotemplate-induced protein crystals in glycerol solution results in distinct, coherently diffracting domains. Only crystals produced according to the Langmuir-Blodgett (LB) nanotemplate technique reveal in all four proteins being tested (lysozyme, insulin, thaumatin and ribonuclease) domains highly radiation resistant, while the crystals produced by the standard hanging drop crystallization method do not. Actually the very same laser exposure causes the disappearance of these "classical" protein crystals during the same time frame of 40 min needed for the laser cutting in all four proteins being tested. The microdiffraction of microcrystals prepered by the combination of Langmuir-Blodgett and Laser technologies proves that not only the Lysozyme survives the process, as shown recently by nanodifraction, but also all three other model proteins appear to behave similarly well, namely insulin, thaumatin and ribonuclease. The result confirms the emerging of a new biophysical technique uniquely usefull for synchrotron radiation studies based on small protein microcrystals uniquely radiation resistant when prepered by LB nanotemplate and subsequently fragmented by Laser.