Laser-Microdissection of Protein Crystals Down to Submicron DimensionsEugenia Pechkova1,2, Luca Belmonte1, Christian Riekel3, Dmitri Popov4, Christian Koenig5 and Claudio Nicolini2*
- *Corresponding Author:
- Claudio Nicolini
Nanoworld Institute, Fondazione ELBA Nicolini
Pradalunga, Bergamo, 24029, Italy
E-mail: [email protected]
Received Date: September 24, 2013; Accepted Date: October 29, 2013; Published Date: October 31, 2013
Citation: Pechkova E, Belmonte L, Riekel C, Popov D, Koenig C, et al. (2013) Laser-Microdissection of Protein Crystals Down to Submicron Dimensions. J Nanomed Nanotechol S15:002. doi:10.4172/2157-7439.S15-002
Copyright: © 2013 Pechkova E. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
We studied laser-microdissection of standard and Langmuir-Blodgett (LB) nanotemplate protein crystals in glycerol solution. The time required for microdissection was significantly longer for LB-crystals as compared to standardcrystals which also more rapidly dissolve. Microfragmentation of lysozyme crystals was observed after extended solvent exposure. Synchrotron radiation nanobeam mapping allowed localizing and aligning cryofrozen lysozyme microfragments. 3D data-sets obtained from two microfragments were refined to atomic resolution. The well-defined electron density maps showed no evidence for damage of radiation of sensitive side-groups. Our results suggest applications of laser-microdissection techniques in structural studies on crystals with a high mosaicity. They also provide a new window for the characterization of protein crystal organization down to the submicron scale, pointing to a new emerging biophysical technique.