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In the world of multimedia, image quality can make or break the viewing experience. But when it comes to biomolecular imaging, clarity is even more crucial—small improvements in resolution can lead to major breakthroughs in understanding proteins, cells, and other biological structures. Now, researchers have introduced a powerful new method that enhances the precision of molecular imaging, opening the door to more accurate insights into molecular dynamics.

Scientists have long used high-resolution imaging to observe single molecules and their nanoscale behavior. However, distinguishing between two fluorescent molecules—known as dipole emitters—that emit light simultaneously from nearly the same point in space has proven notoriously difficult. This challenge has limited researchers’ ability to measure how these molecules are oriented and how they interact, particularly in dense, crowded environments like inside living cells.

A new study published in Physical Review Letters by Matthew Lew, associate professor of electrical and systems engineering at Washington University in St. Louis, and graduate student Yiyang Chen, demonstrates that current polarization imaging techniques cannot differentiate between two coincident dipole emitters and a single molecule. This limitation arises because the emitted light patterns are mathematically indistinguishable.

To overcome this, Lew and Chen combined two complementary techniques: they manipulated the polarization of the laser used to illuminate the sample and measured the polarization of the emitted fluorescence. By fusing these two approaches, they created a method that successfully distinguishes between one and two molecules, even when they are extremely close together.

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This new technique significantly improves measurement precision. It enhances the accuracy of dipole orientation detection by 50% and boosts the precision of angular separation measurements between molecules by up to four times compared with traditional methods.

“Structure always determines function,” Chen explained. “The behavior of cells is governed by the shape and orientation of proteins and biomolecules. For example, antibodies and viral antigens must align in a certain way to interact—these small details at the nanoscale influence how the entire system functions.”

Initially, the researchers assumed existing polarization microscopes could resolve two nearby fluorescent molecules by analyzing the polarization of their emitted light. But their calculations showed otherwise. Dipole pairs produce the same light pattern as a single rotating dipole, making them indistinguishable using standard methods.

By introducing polarized illumination into the equation and pairing it with polarization-based fluorescence detection, the team was able to break through this limitation. Their integrated method generates distinct images for single molecules and molecule pairs, enabling clearer and more precise measurements.

“This represents a big leap in a well-established field,” Lew said. “Traditionally, scientists treated fluorescent molecules as simple point sources because it was easier. But at the nanoscale, treating molecules as dipoles—objects with both direction and intensity—is critical for accurate analysis.”

He added that biological molecules aren’t shaped like perfect spheres, and their interactions depend on how they’re oriented. The team’s new imaging method allows researchers to measure these orientations and protein conformations more precisely, which has far-reaching implications.

The approach could dramatically improve our understanding of dynamic molecular processes, especially in live cells where real-time observations are essential. Lew believes this technique could ultimately advance research in areas ranging from protein behavior and drug development to disease diagnostics.

“To move science forward, the details truly matter,” Lew said. “And now we have a new way to see those details more clearly than ever before.”