Chemical Composition of Subway Particles in Seoul, Korea, Determined Using Quantitative Single Particle Analysis

Author(s):  
Hae-Jin Jung ◽  
Sunni Kang ◽  
Hye Kyeong Kim ◽  
Chul-Un Ro
2011 ◽  
Vol 11 (14) ◽  
pp. 7027-7044 ◽  
Author(s):  
C.-H. Jeong ◽  
M. L. McGuire ◽  
K. J. Godri ◽  
J. G. Slowik ◽  
P. J. G. Rehbein ◽  
...  

Abstract. Mass concentrations of sulphate, nitrate, ammonium, organic carbon (OC), elemental carbon (EC) were determined from real time single particle data in the size range 0.1–3.0 μm measured by an Aerosol Time-of-Flight Mass Spectrometer (ATOFMS) at urban and rural sites in Canada. To quantify chemical species within individual particles measured by an ATOFMS, ion peak intensity of m/z −97 for sulphate, −62 for nitrate, +18 for ammonium, +43 for OC, and +36 for EC were scaled using the number and size distribution data by an Aerodynamic Particle Sizer (APS) and a Fast Mobility Particle Sizer (FMPS). Hourly quantified chemical species from ATOFMS single-particle analysis were compared with collocated fine particulate matter (aerodynamic diameter < 2.5 μm, PM2.5) chemical composition measurements by an Aerosol Mass Spectrometer (AMS) at a rural site, a Gas-Particle Ion Chromatograph (GPIC) at an urban site, and a Sunset Lab field OCEC analyzer at both sites. The highest correlation was found for nitrate, with correlation coefficients (Pearson r) of 0.89 (ATOFMS vs. GPIC) and 0.85 (ATOFMS vs. AMS). ATOFMS mass calibration factors, determined for the urban site, were used to calculate mass concentrations of the major PM2.5 chemical components at the rural site near the US border in southern Ontario. Mass reconstruction using the ATOFMS mass calibration factors agreed very well with the PM2.5 mass concentrations measured by a Tapered Element Oscillating Microbalance (TEOM, r = 0.86) at the urban site and a light scattering monitor (DustTrak, r = 0.87) at the rural site. In the urban area nitrate was the largest contributor to PM2.5 mass in the winter, while organics and sulphate contributed ~64 % of the summer PM2.5 in the rural area, suggesting a strong influence of regional/trans-boundary pollution. The mass concentrations of five major species in ten size-resolved particle-types and aerosol acidity of each particle-type were determined for the rural site. On a mass basis sulphate and OC rich particle-types (OC-S and OC-S-N) accounted for up to 59 % of the particles characterized and aerosols were weakly acidic in the rural area. This is the first study to estimate hourly quantitative data of sulphate, nitrate, ammonium, OC and EC in ambient particles from scaled ATOFMS single particle analysis; these were closely comparable with collocated high time resolution data of sulphate, nitrate and ammonium detected by AMS and GPIC.


2021 ◽  
Vol 27 (S1) ◽  
pp. 1330-1332
Author(s):  
Zuzana Hlavenková ◽  
Dimple Karia ◽  
Miloš Malínský ◽  
Daniel Němeček ◽  
Fanis Grollios ◽  
...  

2001 ◽  
Vol 32 ◽  
pp. 873-874
Author(s):  
S. TOHNO ◽  
S. HAYAKAWA ◽  
A. NAKAMURA ◽  
A. HAMAMOTO ◽  
M. SUZUKI ◽  
...  

2021 ◽  
pp. 107695
Author(s):  
C.O.S. Sorzano ◽  
D. Semchonok ◽  
S.-C. Lin ◽  
Y.-C. Lo ◽  
J.L. Vilas ◽  
...  

Author(s):  
Laura Y. Kim ◽  
William J. Rice ◽  
Edward T. Eng ◽  
Mykhailo Kopylov ◽  
Anchi Cheng ◽  
...  

2013 ◽  
Vol 135 (39) ◽  
pp. 14528-14531 ◽  
Author(s):  
Andrew P. Ault ◽  
Timothy L. Guasco ◽  
Olivia S. Ryder ◽  
Jonas Baltrusaitis ◽  
Luis A. Cuadra-Rodriguez ◽  
...  

2018 ◽  
Vol 294 (5) ◽  
pp. 1602-1608 ◽  
Author(s):  
Xiunan Yi ◽  
Eric J. Verbeke ◽  
Yiran Chang ◽  
Daniel J. Dickinson ◽  
David W. Taylor

Cryo-electron microscopy (cryo-EM) has become an indispensable tool for structural studies of biological macromolecules. Two additional predominant methods are available for studying the architectures of multiprotein complexes: 1) single-particle analysis of purified samples and 2) tomography of whole cells or cell sections. The former can produce high-resolution structures but is limited to highly purified samples, whereas the latter can capture proteins in their native state but has a low signal-to-noise ratio and yields lower-resolution structures. Here, we present a simple, adaptable method combining microfluidic single-cell extraction with single-particle analysis by EM to characterize protein complexes from individual Caenorhabditis elegans embryos. Using this approach, we uncover 3D structures of ribosomes directly from single embryo extracts. Moreover, we investigated structural dynamics during development by counting the number of ribosomes per polysome in early and late embryos. This approach has significant potential applications for counting protein complexes and studying protein architectures from single cells in developmental, evolutionary, and disease contexts.


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