Bruker 600 MHz AVANCE III NMR Spectrometer with Cryoprobe

• Optimized for very high ¹³C sensitivity and very good 1H performance
• Operates with a 5mm cryogenic probe
• Includes a sample case that holds 24 samples
• Has temperature range limits for data collection ranging from 10°to 50°C
• Has remote data collection capabilities. Please email Hyun Lee (danielhl@uic.edu) if you would like to have remote data collection capability
• Reservation: available 24 hours/day Mon-Sun
  • Minimum reservation: 30 minutes
  • Time increment: 30 minutes
  • Maximum reservation at a time: 48 hours

Beamline 21-ID-D

• Fully tunable beamline (6–20 keV) with Kohzu monochromator and bimorph mirrors
• Has a new DECTRIS EIGER2 16M
• The flux on 21-ID-D is roughly an order of magnitude stronger than the side stations, necessitating the EIGER2 ability for dual readout to prevent saturation

Beamline 21-ID-F & Beamline 21-ID-G

• Fixed-wavelength stations (~0.9786 Å) above the Se peak and ideal for routine SAD
• All three stations are being upgraded to have Arinax MD3-UP microdiffractometers along with Pixel Array Detectors
• 21-ID-F a DECTRIS EIGER 9M, and 21-ID-G has a DECTRIS PILATUS 6M on loan from the original SBC-CAT, Sector 19.
• New sample changers will hold 37 UniPucks and eventually support fully automated data collection.

Beamline Status Update

• 21-ID-G is currently available for remote and on-site collection with the original CATS sample changer supporting SPINE baskets and a MarMosaic 300 CCD detector
• 21-ID-F is available for on-site collection with an EIGER 9M PAD
• 21-ID-D is largely dismantled during its upgrade this summer with some serial crystallography experiments being performed in parallel

600 NMR Data Acquisition

600 NMR Data Acquisition Service by staff is available.

Training

• Bruker 600 MHz NMR for new users
• Bruker 600 MHz NMR for COP or Chemistry NMR users

X-ray Crystallography

The Structural Biology Core supports research projects requiring macromolecular structure determination and biophysical characterization through X-ray crystallography. Investigators may submit concentrated protein samples (10–15 mg/mL) for crystallization screening. If protein purification is also needed, please submit a “Protein Purification Service” request through the Biophysics Core on iLab, providing detailed information and specifying your starting point for the X-ray crystallography workflow.

Please note that data analysis and sample setup timelines may vary significantly depending on sample quality and project complexity. For consultation, please contact Dr. Hyun Lee (danielhl@uic.edu) or Val Yu (qihyu@uic.edu).