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Updated: Jun 6, 2026

Crystallization and Structural Determination of an Enzyme:Substrate Complex by Serial Crystallography in a Versatile Microfluidic Chip
Published on: March 20, 2021
Crystallization and preliminary X-ray analysis of a novel esterase Rv0045c from Mycobacterium tuberculosis
Lipeng Xu1, Jiubiao Guo, Xiangdong Zheng
1School of Medicine, Tsinghua University, Beijing 100084, People's Republic of China.
Abstract:
The Rv0045c protein is predicted to be an esterase that is involved in lipid metabolism in Mycobacterium tuberculosis. The protein was overproduced in Escherichia coli, purified and crystallized using the hanging-drop vapour-diffusion method. The Rv0045c protein crystals diffracted to a resolution of 2.7 Å using a synchrotron-radiation source and belonged to space group P3(1) or P3(2), with unit-cell parameters a=b=73.465, c=48.064 Å, α=β=90, γ=120°. Purified SeMet-labelled Rv0045c protein was also crystallized and formed crystals that diffracted to a resolution of 3.0 Å using an in-house X-ray radiation source.
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