Crystallization and preliminary crystallographic analysis of the Escherichia coli water channel AqpZ
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Updated: Aug 26, 2026

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies
Published on: November 20, 2021
Brenda V Daniels1, Jian-Sheng Jiang, Dax Fu
1Biology Department, Brookhaven National Laboratory, Upton, NY 11973-5000, USA.
Abstract:
AqpZ is a 24 kDa integral membrane protein that facilitates water movement across the plasma membrane of Escherichia coli. In this study, the first crystallization and preliminary X-ray analysis of AqpZ are described. AqpZ was overexpressed and purified with a yield of 13 mg of purified AqpZ per litre of cell culture. The purified AqpZ was shown to be a monodisperse species consisting of tetrameric protein-detergent complexes. A crystallization condition for producing diffraction-quality crystals was identified. Initial X-ray analysis indicated that the diffraction limit of AqpZ extended to 3.6 A. Crystals were found to belong to space groups P4(1)22 or P4(3)22, with unit-cell parameters a = b = 119.04, c = 380.23 A.

