X-ray Crystallography Facility

The X-ray Crystallography facility is located on the 2nd floor of BioTech One in VCU’s Center for Drug Discovery. The facility provides investigators equipment and resources for crystallographic analysis of macromolecules and/or small molecules. The facility operates a state-of-the-art Rigaku MicroMax-007HF X-ray Generator with VariMax-HF Arc Optics/Hybrid Photon Counter, Eiger R 4M Detector and AFC11 Goniometer, Rigaku Gryphon Crystallization Robot, Rigaku Alchemist Liquid Handling System, Crystallization Incubators, and Rigaku Minstrel/Gallery Imaging System.  

The crystallography facility operates as a full-service core by performing crystallization, X-ray diffraction data collection processing, phasing, crystallographic refinement, model building, and visualization. The structural data obtained by the core will provide scientists with a wealth of information including but not limited to 3D-structure, biological functions, structure-based drug design, ligand or DNA binding to protein, mutational effect of target macromolecules, and absolute stereochemistry of chiral compounds. The facility is complemented by a variety of training and service offerings. In addition to serving the VCU community, we also offer crystallography services to outside organizations. Please contact us for your crystallographic and other structural biology service needs.

Services

• Feasibility determination/studies
• Crystallization of small molecules and macromolecules
• Characterization of crystals
• Diffraction data collection at ambient temperature and 100K
• Data analysis and processing
• Structure determination and analysis

Note: All users must be appropriately trained prior to using the X-ray instrument and other equipment, including appropriate radiation safety measures. If you need training please email Faik Musayev, Ph.D. or call (804) 828-4875.

Equipment and resources

• Rigaku Gryphon Crystallization Robot
• Rigaku Alchemist Liquid Handling System
• Rigaku Minstrel/Gallery Imaging
• Crystallization Incubators
• CrysCam Digital Microscope for monitoring crystal growth and manipulation
• Olympus SZ51 and Nikon SMZ-2T Microscopes
• Rigaku MicroMax-007HF X-ray Generator with VariMax-HF Arc Optics/Hybrid
• Photon Counter, Eiger R 4M Detector and AFC11 Goniometer VariMax-HF Arc optics
• Oxford Cobra Cryo-system for data collection at 100K
• NitroFlowLab Nitrogen Generator
• Computational facilities for diffraction data collection, processing and structure determination
• Crystallographic and modeling software packages

Reservation

X-ray time request (login or register to have login access)

Reserve the instrument

• All users must be appropriately trained prior to using the X-ray instrument and other equipment, including appropriate radiation safety measures. If you need training and/or help to operate the instrument, please contact Faik Musayev, Ph.D.. 
• First-time users require radiation safety training prior to operating the X-ray instrument. Note that this applies to only VCU researchers. All crystallographic services for outside organizations are performed by our in-house trained personnel and are therefore not required to take the radiation safety training. The radiation safety online training is offered through SciShield. To enroll in this course, login to SciShield and select "Training" then "Course directory". Then, search for the course "Research X-ray radiation safety training" and choose "Launch course". Visit the Radiation safety guide to learn more.

Publications (selected)

1. Tramonti A, Donkor AK, Parroni A, Musayev FN, Barile A, Ghatge MS, Graziani C, Alkhairi M, AlAwadh M, di Salvo ML, Safo MK, Contestabile R.  Functional and structural properties of pyridoxal reductase (PdxI) from Escherichia coli: a pivotal enzyme in the vitamin B6 salvage pathway. FEBS J. 2023, 290 (23): 5628-5651.
2. Tramonti A, Ghatge MS, Babor JT, Musayev FN, di Salvo ML, Barile A, Colotti G, Giorgi A, Paredes SD, Donkor AK, Al Mughram MH, de Crécy-Lagard V, Safo MK, Contestabile R. Characterization of the Escherichia coli pyridoxal 5'-phosphate homeostasis protein (YggS): Role of lysine residues in PLP binding and protein stability. Protein Sci. 2022, 31(11): e4471. doi: 10.1002/pro.4471.
3. Huang B, Ghatge MS, Donkor AK, Musayev FN, Deshpande TM, Al-Awadh M, Alhashimi RT, Zhu H, Omar AM, Telen MJ, Zhang Y, McMahon TJ, Abdulmalik O, Safo MK. Design, Synthesis, and Investigation of Novel Nitric Oxide (NO)-Releasing Aromatic Aldehydes as Drug Candidates for the Treatment of Sickle Cell Disease. Molecules. 2022, 27(20): 6835. doi: 10.3390/molecules27206835.
4. Alhashimi RT, Ghatge MS, Donkor AK, Deshpande TM, Anabaraonye N, Alramadhani D, Danso-Danquah R, Huang B, Zhang Y, Musayev FN, Abdulmalik O, Safo MK. Design, Synthesis, and Antisickling Investigation of a Nitric Oxide-Releasing Prodrug of 5HMF for the Treatment of Sickle Cell Disease. Biomolecules. 2022, 12(5): 696. doi: 10.3390/biom12050696.
5. Li H, Musayev FN, Yang J, Su J, Liu Q, Wang W, Fang X, Zhou L, Liu Q.  A novel and unique ATP hydrolysis to AMP by a human Hsp70 Binding immunoglobin protein (BiP)  Protein Sci. 2022 Apr;31(4):797-810. doi: 10.1002/pro.4267. Epub 2021 Dec 31
6. Demers M, Sturtevant S, Guertin KR, Gupta D, Desai K, Vieira BF, Li W, Hicks A, Ismail A, Gonçalves BP, Di Caprio G, Schonbrun E, Hansen S, Musayev FN, Safo MK, Wood DK, Higgins JM, Light DR. MetAP2 inhibition modifies hemoglobin S to delay polymerization and improves blood flow in sickle cell disease. Blood Adv. 2021, 5(5):1388-1402. doi: 10.1182/bloodadvances.2020003670. PMID: 33661300