About me

Jingjing Zhao is a PhD student at the Department of Materials and Environmental Chemistry (MMK) at Stockholm University. She received her Bachelor's degree in Physics in 2012 at Xiangtan University and Master's degree in Materials Science and Engineering in 2015 at the University of Science and Technology of China (USTC). Her research involves method development and structure determination of beam-sensitive materials (proteins and porous materials) by electron crystallography.

Publications

A selection from Stockholm University publication database

• Article A metal-organic framework for efficient water-based ultra-low-temperature-driven cooling
  2019. Dirk Lenzen (et al.). Nature Communications 10

  Efficient use of energy for cooling applications is a very important and challenging field in science. Ultra-low temperature actuated (T-driving< 80 degrees C) adsorption-driven chillers (ADCs) with water as the cooling agent are one environmentally benign option. The nanoscale metal-organic framework [Al(OH)(C6H2O4S)] denoted CAU-23 was discovered that possess favorable properties, including water adsorption capacity of 0.37 g(H2O)/g(sorbent) around p/p(0 )= 0.3 and cycling stability of at least 5000 cycles. Most importantly the material has a driving temperature down to 60 degrees C, which allows for the exploitation of yet mostly unused temperature sources and a more efficient use of energy. These exceptional properties are due to its unique crystal structure, which was unequivocally elucidated by single crystal electron diffraction. Monte Carlo simulations were performed to reveal the water adsorption mechanism at the atomic level. With its green synthesis, CAU-23 is an ideal material to realize ultra-low temperature driven ADC devices.

• Article Solving a new R2lox protein structure by microcrystal electron diffraction
  2019. Hongyi Xu (et al.). Science Advances 5 (8)

  Microcrystal electron diffraction (MicroED) has recently shown potential for structural biology. It enables the study of biomolecules from micrometer-sized 3D crystals that are too small to be studied by conventional x-ray crystallography. However, to date, MicroED has only been applied to redetermine protein structures that had already been solved previously by x-ray diffraction. Here, we present the first new protein structure-an R2lox enzyme-solved using MicroED. The structure was phased by molecular replacement using a search model of 35% sequence identity. The resulting electrostatic scattering potential map at 3.0-angstrom resolution was of sufficient quality to allow accurate model building and refinement. The dinuclear metal cofactor could be located in the map and was modeled as a heterodinuclear Mn/Fe center based on previous studies. Our results demonstrate that MicroED has the potential to become a widely applicable tool for revealing novel insights into protein structure and function.

Show all publications by Jingjing Zhao at Stockholm University