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Altissimo M, Kiskinova M, Mincigrucci R, et al. Perspective: A toolbox for protein structure determination in physiological environment through oriented, 2D ordered, site specific immobilization. Struct Dyn. 2017;4(4):044017doi: 10.1063/1.4981224.
Altissimo, M., Kiskinova, M., Mincigrucci, R., Vaccari, L., Guarnaccia, C., & Masciovecchio, C. (2017). Perspective: A toolbox for protein structure determination in physiological environment through oriented, 2D ordered, site specific immobilization. Structural dynamics (Melville, N.Y.), 4(4), 044017. https://doi.org/10.1063/1.4981224
Altissimo, M, et al. "Perspective: A toolbox for protein structure determination in physiological environment through oriented, 2D ordered, site specific immobilization." Structural dynamics (Melville, N.Y.) vol. 4,4 (2017): 044017. doi: https://doi.org/10.1063/1.4981224
Altissimo M, Kiskinova M, Mincigrucci R, Vaccari L, Guarnaccia C, Masciovecchio C. Perspective: A toolbox for protein structure determination in physiological environment through oriented, 2D ordered, site specific immobilization. Struct Dyn. 2017 Apr 14;4(4):044017. doi: 10.1063/1.4981224. eCollection 2017 Jul. PMID: 28428974; PMCID: PMC5392127.
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Struct Dyn. 2017 Apr 14;4(4):044017. doi: 10.1063/1.4981224. eCollection 2017 Jul.

Perspective: A toolbox for protein structure determination in physiological environment through oriented, 2D ordered, site specific immobilization.

Structural dynamics (Melville, N.Y.)

M Altissimo, M Kiskinova, R Mincigrucci, L Vaccari, C Guarnaccia, C Masciovecchio

Affiliations

  1. Elettra Sincrotrone Trieste, S. S. 14?km 163, 34149 Trieste, Basovizza, Italy.
  2. International Centre for Genetic Engineering and Biotechnology, Padriciano 99, 34149 Trieste, Italy.

PMID: 28428974 PMCID: PMC5392127 DOI: 10.1063/1.4981224

Abstract

Revealing the structure of complex biological macromolecules, such as proteins, is an essential step for understanding the chemical mechanisms that determine the diversity of their functions. Synchrotron based X-ray crystallography and cryo-electron microscopy have made major contributions in determining thousands of protein structures even from micro-sized crystals. They suffer from some limitations that have not been overcome, such as radiation damage, the natural inability to crystallize a number of proteins, and experimental conditions for structure determination that are incompatible with the physiological environment. Today, the ultra-short and ultra-bright pulses of X-ray free-electron lasers have made attainable the dream to determine protein structures before radiation damage starts to destroy the samples. However, the signal-to-noise ratio remains a great challenge to obtain usable diffraction patterns from a single protein molecule. With the perspective to overcome these challenges, we describe here a new methodology that has the potential to overcome the signal-to-noise-ratio and protein crystallization limits. Using a multidisciplinary approach, we propose to create ordered, two dimensional protein arrays with defined orientation attached on a self-assembled-monolayer. We develop a literature-based flexible toolbox capable of assembling different kinds of proteins on a functionalized surface and consider using a graphene cover layer that will allow performing experiments with proteins in physiological conditions.

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