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Aquaporins

Aquaporins

Aquaporins or AQPs are a family of integral membrane proteins whose primary function is to transport water, while some called aquaglyceroporins also transport glycerol. In addition, aquaporins have also been suspected to be involved in transporting volatile substances, such as carbon dioxide and ammonia, across membranes. Such AQPs that act as gas channels are often highly expressed in cells involved in the gaseous exchange, such as red blood cells, epithelial cells, and pulmonary capillaries.

Cryo-electron Microscopy

Cryo-electron Microscopy

Conventional electron microscopy (EM) involves dehydration, fixation, and staining of biological samples, which distorts the native state of biological molecules and results in several artifacts. Also, the high-energy electron beam damages the sample and makes it difficult to obtain high-resolution images. These issues can be addressed using cryo-EM, which uses frozen samples and gentler electron beams. The technique was developed by Jacques Dubochet, Joachim Frank, and Richard Henderson, for...

X-ray Crystallography

X-ray Crystallography

The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
Diffraction
Diffraction is the change in the direction of travel experienced by an electromagnetic wave when it encounters a physical barrier whose dimensions are comparable to those of the wavelength of the light. X-rays are electromagnetic radiation with wavelengths about as long as the distance between neighboring...

Determination of Crystal Structures

Determination of Crystal Structures

In the late 1800s, the revelation that light extended beyond visible wavelengths led to the discovery of X-rays by Wilhelm Roentgen. Recognized as high-energy electromagnetic radiation with short wavelengths, X-rays prompted exploration into their interaction with crystals. Max von Laue proposed in 1912 that the periodic arrangement of atoms, ions, or molecules in crystals would cause them to diffract X-rays, a hypothesis confirmed through experiments with copper sulfate and zinc sulfide...

Ionic Crystal Structures

Ionic Crystal Structures

Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size.
Most monatomic ions behave as charged spheres, and their attraction for ions of opposite charge is the same in every direction. Consequently, stable structures for ionic compounds result (1) when ions of one charge are surrounded by as many ions as possible of the opposite...

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Related Experiment Video

Updated: Jun 8, 2026

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

Sample Preparation using a Lipid Monolayer Method for Electron Crystallographic Studies

Published on: November 20, 2021

Electron crystallography and aquaporins.

Andreas D Schenk¹, Richard K Hite, Andreas Engel

¹Department of Cell Biology, Harvard Medical School, Boston, Massachusetts, USA.

Methods in Enzymology

|October 5, 2010

Summary

Electron crystallography reveals near-atomic structures of aquaporins (AQPs), advancing membrane protein research. This technique also benefits from AQP structural studies, driving innovation in electron crystallography methods.

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Area of Science:

Structural biology
Biophysics
Membrane protein research

Background:

Electron crystallography provides near-atomic resolution structures of membrane proteins.
Aquaporins (AQPs) are crucial membrane proteins forming pores for water and solute transport.
Bacteriorhodopsin was an early target for electron crystallography.

Purpose of the Study:

To summarize insights from electron crystallography on aquaporin biology.
To describe technical advancements in electron crystallography driven by AQP studies.
To discuss lessons learned from electron crystallographic work on AQPs.

Main Methods:

Electron crystallography of two-dimensional (2D) crystals.
Structural analysis of membrane proteins.
Investigating water and solute transport mechanisms.

Main Results:

Electron crystallography has elucidated AQP structures, enhancing understanding of their function.
Structural studies on AQPs have spurred technical developments in electron crystallography.
Insights into AQP biology have been gained through high-resolution structural data.

Conclusions:

Electron crystallography is a powerful tool for studying membrane proteins like AQPs.
The interplay between AQP research and electron crystallography has led to mutual advancements.
Lessons learned from AQP studies offer valuable guidance for future electron crystallography applications.