X-Ray Department 2017-08-23T22:35:11+00:00
Microdiffraction beamline NYX at NSLS-II

NYSBC’s new, next-generation beamline, NYX, will replace our previous beamlines, X4A and X4C. It is designed to utilize the brightness of the NSLS-II, the new synchrotron at Brookhaven National Lab that began operations in 2015.

About X-Ray

The X-Ray crystallography department operates beamline NYX, designed and constructed by NYSBC at Brookhaven National Lab’s NSLS-II synchrotron, as well as in-house X-ray sources at NYSBC’s Manhattan facility. Staff in this department use this equipment to collect diffraction data from crystals of biological molecules to determine their 3-dimensional structure. NYX is the successor of NYSBC’s X4A beamline, a pioneer in the application of multiwavelength anomalous diffraction (MAD) analysis to the determination of protein crystal structures.

Applications

Macromolecular complexes and assemblies
Structures of protein-protein complexes and protein-nucleic acid complexes are essential to decipher the mystery of life at atomic level. Image: complex between two subunits of the bacterial clamp loader β (yellow, purple) and DNA (red); Georgescu et al. Cell 132, 43 (2008)

Membrane Proteins
NYX beamline is optimized for structural analyses of membrane proteins with high relevance in health and diseases. Image: trimeric structure of a bacterial homolog of the SLAC1 anion channel on plant leaves; Chen et al. Nature 467, 1074 (2010)

Microdiffraction
NYX will support routine structure determination of micron-sized crystals. Even with larger or needle crystals, NYX will use micron-sized beam for reduced radiation damage and reduced background. Image: micron-sized crystals of two membrane proteins.

Optimized anomalous signals measurement
NYX will optimize anomalous scattering from heavy atoms at high energy x-ray for MAD/SAD experiments, and from multiple crystals at lower energy x-ray for direct structure determination without heavy atoms. Image: structure of CysZ transporter solved with anomalous diffraction from multiple native protein crystals at lower x-ray energy; Liu et al. Science 336, 1033 (2012)