How NSLS Illuminated the Frontiers of Science
In the heart of Long Island, a remarkable machine once bent the laws of physics to shed light on the atomic secrets of life itself.
Imagine a microscope so powerful it can reveal the intricate architecture of a single protein or trace the atomic landscape of a new battery material. For over three decades, this was the reality at the National Synchrotron Light Source (NSLS) at Brookhaven National Laboratory. A cornerstone of the global scientific community, the NSLS provided the brilliant light that enabled researchers to see the unseen. In 2009, this facility was at the peak of its powers, hosting thousands of scientists whose work would lead to Nobel prizes and technological breakthroughs that shape our world today 1 .
Synchrotron light is an exceptionally intense, focused beam of light—spanning from infrared to X-rays—generated by electrons traveling at nearly the speed of light. At the NSLS, electrons were first accelerated in a linear accelerator, then boosted to higher energies before being injected into one of two storage rings: the X-ray ring or the VUV (vacuum ultraviolet) ring 1 .
As these high-energy electrons curved around the ring, powerful magnets bent their path, causing them to lose energy in the form of photons, or light. This "synchrotron radiation" was anything but ordinary; it was "white light" containing a spectrum of wavelengths.
Electrons accelerated to nearly the speed of light in a linear accelerator and storage rings.
Powerful magnets bend electron paths, causing emission of intense synchrotron radiation.
Specialized beamlines channel light to experimental stations for diverse research applications.
This light was then channeled down specialized beamlines—essentially experimental stations—where monochromators selected specific, precise wavelengths to probe the inner structure of matter 1 . The NSLS was a second-generation synchrotron, a class of machine defined by the pioneering Chasman-Green lattice, a magnetic arrangement that optimized the electron beam for producing this brilliant light 1 .
The NSLS was fundamentally a national user facility, open to researchers from academia, industry, and government through a competitive proposal system 1 . Its impact was immense.
Users in 2009
U.S. States
Countries
Publications
Groundbreaking work done at the NSLS contributed to multiple Nobel Prizes. In 2003, Roderick MacKinnon used it to decipher the structure of a neuronal ion channel. In 2009, Venkatraman Ramakrishnan, Thomas A. Steitz, and Ada E. Yonath relied on NSLS's X-rays to determine the atomic structure of the ribosome 1 .
Scientific Application: Structural Biology, Material Science
What It Reveals: The three-dimensional atomic arrangement of crystals, such as proteins or novel materials.
Scientific Application: Chemistry, Catalysis
What It Reveals: The local chemical structure and environment around a specific element, even in non-crystalline materials.
Scientific Application: Surface Science
What It Reveals: The elemental composition and chemical state of a material's surface.
Scientific Application: Environmental Science, Biology
What It Reveals: The distribution of different chemical components in a sample at a micro- or nano-scale.
The science performed at the NSLS was as diverse as its users. The facility's beamlines enabled a wide range of techniques, from X-ray diffraction that revealed atomic structures to XAFS (X-ray absorption fine structure) that probed the chemical environment of atoms in a material 1 .
One of the most significant achievements linked to the NSLS was the detailed mapping of the ribosome, the cell's protein-making machine. This work, which earned the 2009 Nobel Prize in Chemistry, was a monumental decades-long effort, with the NSLS playing a critical role.
Researchers first had to create high-quality crystals of ribosomes, a formidable challenge given their complex structure.
At the NSLS, these tiny, frozen crystals were placed in the path of the intense, focused X-ray beam. As the X-rays struck the crystal, they diffracted, scattering in a unique pattern.
By collecting and analyzing hundreds of these diffraction patterns from different angles, scientists could work backwards to calculate the exact 3D electron density map—the atomic structure—of the ribosome.
The resulting atomic-scale models showed how the ribosome reads genetic code and synthesizes proteins with extraordinary fidelity. They also revealed how certain antibiotics work by binding to bacterial ribosomes and disrupting their function. This provided a blueprint for designing new and more effective drugs to combat antibiotic-resistant infections.
The ribosome structure determination was a landmark achievement that transformed our understanding of protein synthesis and opened new avenues for antibiotic development.
| Tool/Reagent | Function in the Experiment |
|---|---|
| Protein/Ribosome Crystals | Acts as a natural grating that causes X-rays to diffract, creating the pattern needed to determine atomic structure. |
| Cryogenic Nitrogen Stream | A stream of cold nitrogen gas used to freeze crystals, protecting them from damage by the powerful X-ray beam. |
| Intense Synchrotron X-rays | Provides the high-brightness, tunable light required to probe the electronic and atomic structure of matter. |
| X-ray Detector | A highly sensitive camera that records the diffraction patterns produced when X-rays interact with the crystal. |
| Computational Software | Complex algorithms that transform hundreds of 2D diffraction patterns into a coherent 3D atomic model. |
The original NSLS performed its last experiment on September 30, 2014, after more than 30 years of service 1 . But its end marked a brilliant new beginning. Even as the NSLS was running, the NSLS-II was under construction, a next-generation machine designed to produce X-rays 10,000 times brighter than its predecessor 2 .
NSLS-II, which opened in 2015, is a third-generation light source designed to probe materials with nanoscale resolution and exquisite sensitivity 5 . It continues the legacy of its predecessor, providing tools for scientists to tackle the grand challenges of our time, from designing better batteries to understanding biological processes at the molecular level 3 8 .
The story of the NSLS is more than a history of a machine; it is a story of human curiosity and collaboration. It provided the light by which scientists could read the fundamental code of nature, leading to advances in medicine, energy, and technology that continue to benefit society. Its brilliant legacy shines on, illuminating the path for future discovery.