Dataset Information

Single-Molecule Fluorescence Microscopy Reveals Local Diffusion Coefficients in the Pore Network of an Individual Catalyst Particle.

ABSTRACT: We used single-molecule fluorescence microscopy to study self-diffusion of a feedstock-like probe molecule with nanometer accuracy in the macropores of a micrometer-sized, real-life fluid catalytic cracking (FCC) particle. Movies of single fluorescent molecules allowed their movement through the pore network to be reconstructed. The observed tracks were classified into three different states by machine learning and all found to be distributed homogeneously over the particle. Most probe molecules (88%) were immobile, with the molecule most likely being physisorbed or trapped; the remainder was either mobile (8%), with the molecule moving inside the macropores, or showed hybrid behavior (4%). Mobile tracks had an average diffusion coefficient of D = 8 × 10-14 ± 1 × 10-13 m2 s-1, with the standard deviation thought to be related to the large range of pore sizes found in FCC particles. The developed methodology can be used to evaluate, quantify and map heterogeneities in diffusional properties within complex hierarchically porous materials.

SUBMITTER: Hendriks FC

PROVIDER: S-EPMC5632810 | biostudies-literature | 2017 Oct

REPOSITORIES: biostudies-literature

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Single-Molecule Fluorescence Microscopy Reveals Local Diffusion Coefficients in the Pore Network of an Individual Catalyst Particle.

Hendriks Frank C FC Meirer Florian F Kubarev Alexey V AV Ristanović Zoran Z Roeffaers Maarten B J MBJ Vogt Eelco T C ETC Bruijnincx Pieter C A PCA Weckhuysen Bert M BM

Journal of the American Chemical Society 20170913 39

We used single-molecule fluorescence microscopy to study self-diffusion of a feedstock-like probe molecule with nanometer accuracy in the macropores of a micrometer-sized, real-life fluid catalytic cracking (FCC) particle. Movies of single fluorescent molecules allowed their movement through the pore network to be reconstructed. The observed tracks were classified into three different states by machine learning and all found to be distributed homogeneously over the particle. Most probe molecules ...[more]

PMID: 28902508

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Project description:The protein is naturally dynamic and heterogeneous in solution. Protein dynamics involves both equilibrium fluctuations that regulate biological function and other non-equilibrium effects of biological motors, which convert chemical energy to mechanical energy. However, a single, unique structure of protein determined from X-ray crystal and conventional single-particle electron microscopy is insufficient to encompass the dynamic nature of proteins in solution. Structure determination of dynamic and heterogeneous protein is essentially required the determination of each individual particle of protein. Recently, Drs. Gang Ren and Lei Zhan published the first single molecule three-dimensional (3D) EM images of individual proteins ever obtained with enough clarity to determine their structure, an IgG antibody (14 Å resolution) and a 17nm HDL (36 Å resolution). These results depended upon four innovations: i) improved cryo-electron microscopy (cryoEM) sample preparation and Electron microscopy (EM) operation conditions resulted in the successful imaging of a 17 nm HDL particle (120-200kDa) by cryo-electron tomography (cryoET); ii) developed an optimized NS (OpNS) protocol that eliminates the rouleau artifact that has plagued EM research for three decades. This OpNS protocol provides high-contrast single lipoprotein images with similar size (<5%) and shape (<5%) to that seen by cryoEM; iii) developed a high-resolution and high contrast sample preparation protocol, cryo-positive-staining (cryoPS) that allows direct visualization of the secondary structure of a small protein, such as the β-strands in CETP and the helical double belt of apoA-I in spherical HDL; iv) developed a robust tomography reconstruction method, Individual Particle Electron Tomography (IPET) that is a high-resolution, high throughput reconstruction method that, to the best of our knowledge, is the only method for determining an individual protein structure. Remarkably, IPET went against the conventional wisdom that a single protein can NOT be reconstructed by EM and this opens a door for the study of protein dynamics via a particle-by-particle structural comparison.

Dataset Information

Single-Molecule Fluorescence Microscopy Reveals Local Diffusion Coefficients in the Pore Network of an Individual Catalyst Particle.

Publications

Single-Molecule Fluorescence Microscopy Reveals Local Diffusion Coefficients in the Pore Network of an Individual Catalyst Particle.

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