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Novel millisecond time resolved structural biology and imaging research using footprinting technology is carried out at synchrotron beamline X28 of the National Synchrotron Light Source. A stopped flow device is used to poise macromolecules in these imaging studies.

Center for Synchrotron Biosciences

Contents

• Contact Information
• Grant Number
• Research Emphasis
• Current Research
• Resource Capabilities
• References 

Contact Information

Grant Number

Research Emphasis

Current Research

• Structural genomics, actin cytoskeleton dynamics, folding and dynamics of ribozymes, DNA-protein interactions, protein folding.
• Development of millisecond hydroxyl-radical footprinting techniques coupled to stopped-flow devices.

Resource Capabilities

Beamlines and Facilities at the National Synchrotron Light Source

• Beamline X9B delivering 5-15 keV x-rays for X-ray Spectroscopy including High Count Rate Solid State Detector and Diplex Cryostat for low temperature studies
• Beamline X9A delivering 5-15 keV x-rays for Macromolecular Crystallography including MAR 165 mm CCD Detector
• Beamline U2B delivering 30-5000 cm^-1 light for Infrared Microscopy and Infrared Imaging including rapid mixing apparatus, far-infrared chamber, and cryostat
• Beamline X28C delivering "white" x-rays 5-15 keV for synchrotron footprinting including stopped flow devices
• Beamline X29 Undulator delivering 5-15 keV x-rays for Macromolecular Crystallography including ADSC 315 Detector
• Biochemistry laboratory and cold room located at NSLS
• Thermo-Finnegan Classic Mass Spectrometer coupled with Waters LC

Facilities at the Case Western Reserve University School of Medicine

• Thermo-Finnegan Deca-XP Mass Spectrometer with nanospray capabilities coupled to Dionex capillary LC
• Thermo-Finnegan Fourier Transform LTQ mass spectrometer with 2 ppm resolution for top-down and bottom-up proteomics capabilities operated with Dionex capillary LC system; a 96-well autosampler and switcher is utilized with this system
• GE/Amersham 2-D Gel DICE system with robotic spot picking
• Two Applied Biosystems Q-star mass spectrometers with Dionex capillary LC system - one with electrospray and the other with MALDI source
• Thermo-Finnegan DECA XP-Plus and LTQ instruments, both with nanospray capability
• Beckman Biomec FX robotic liquid handling systems with 96-well head and SPAN-8 flexible arm.  Numerous ALPs are available including heating and cooling and vacuum filtration.

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References

1. Brenowitz M, Chance MR, Dhavan G, Takamoto K. Probing the structural dynamics of nucleic acid structure by quantitative time-resolved and equilibrium hydroxyl radical "footprinting". Curr. Opin. Struct. Biol. 2002;12:648-653.
2. Takamoto K, He Q, Morris S, Chance MR, Brenowitz M. Monovalent cations mediate formation of native tertiary structure of the tetrahymena thermophila ribozyme: implications for the kinetics of folding. Nat. Stru. Biol. 2002;9:928-933.
3. Kiselar JG, Janmey P, Almo SC, Chance MR. Visualizing the Ca⁺² Dependent activation of gelsolin using synchrotron footprinting. Proc. Nat. Acad. Sci. (USA) 2003;100:3942-3947.
4. Guan JG, Almo SC, Chance MR. Synchrotron radiolysis and mass spectrometry: a new approach to research on the actin cytoskeleton. Acct. Chem. Res. 2004;37:221-229.
5. Gupta S, Mangel WF, Baniecki ML, McGrath WJ, Takamoto K, Chance MR. DNA binding provides a molecular strap activating the Adenovirus Proteinase. Mol. & Cell. Proteomics 2004;3:950-959.
6. Chance MR, Fiser A, Sali A, Pieper U, Eashwar N, Xu G, Radahakanan T, Marinkovic N. High throughput computational and experimental techniques in structural genomics. Genome Research 2004;14:2145-2154.
7. Xu G, Liu R, Zak O, Aisen P, Chance MR. Structural allostery and binding of the transferrin-receptor complex.
   Mol Cell Proteomics. 2005 Sep 16; [Epub ahead of print].
8. Guan JQ, Chance MR. Structural proteomics of macromolecular assemblies using oxidative footprinting and mass spectrometry.
   Trends Biochem Sci. 2005 Oct;30(10):583-92. 
9. Brenowitz M, Erie DA, Chance MR. Catching RNA polymerase in the act of binding: intermediates in transcription illuminated by synchrotron footprinting. Proc Natl Acad Sci U S A. 2005 Mar 29;102(13):4659-60.