PROJECT SUMMARY/ ABSTRACT The X-ray diffraction system, in the laboratory of Prof. Joshua Sakon (PI X-ray crystallography core), has played and will continue to play a key role in the statewide research efforts in the structure determination of biomolecules. His involvement in the Arkansas INBRE began in 2001 when the Arkansas BRIN was first funded through a grant from the National Center for Research Resources. Dr. Sakon co-directs the Biotechnology Core and in that role helps Arkansas INBRE network faculty and students access University of Arkansas core facilities. This budget is for the acquisition of the HyPix-6000HE Hybrid Photon Counting Detector and Universal Kappa 4-Axis Goniometer for the X-Ray diffraction system. The instrumentation will enhance user access to new technology while replacing outdated equipment that is no longer serviceable by the manufacturer. With the new installation, the deinstallation of Saturn-92 and AFC9, Beryllium window of left port will also be required. The system, which was purchased in 2003, has provided an excellent return on investment for 17 years. Eighty-one structures solved in the facility are validated and made accessible from the Protein Data Bank (PDB). The facility provided 78.4% of three-dimensional structures deposited from our state of Arkansas. During the period 2003−2021, the coordinates were frequently downloaded (1,685,267 times) and examined using the website tools implemented by PDB (503,322 times) and led our state in impact (87.9% of downloads and views). These structures are aiding in understanding protein architectures and designing new molecules. The detector/goniometer portion of the system is in desperate need of upgrade. However, the old detector is no longer supported by the manufacturer Replacing the existing detector/goniometer portion of the system will extend the life of the X-ray diffraction system as well as increase the functionality and usability of the system. The new generation X-ray detector will produce higher quality data and the software that now comes with the detector/goniometer replacement will leverage advanced new algorithms developed in recent years and will be capable of extracting more accurate information even with the same signal to noise ratio. The investment will extend the capacity of the instrument from being a system dedicated to protein crystallography to one that is capable of also generating high-quality analytics for small molecules. With the proposed upgrade of the system, for less money than a new small molecule crystallography system, the facility can continue to serve the needs of INBRE-, COBRE-, and as well as other NIH-supported investigators on this campus and across the state.