Skip to main content
Sign In

Xray Crystallography Structural Biology Shared Resource at CU Cancer Center

The X-ray crystallography facility is fully equipped for biomolecular crystallization, crystal screening, data collection, data processing, structure-determination and model building. The Rigaku/MSC Crystallization Robotics include: an Alchemist liquid handling robot for optimization screen production, a Phoenix drop setting robot, and 2 Desktop Minstrel imaging units, and a plate hotel that are all networked and integrated with Crystal trak software. The home source is composed of a Rigaku Micromax 007 high frequency microfocus X-ray generator, a VariMax high flux optic with adjustable divergence, an AFC11 4-axis goniometer, a Pilatus 200K 2D area detector, and an Oxford Cobra cryo-system. HKL-3000R is used for data collection and processing and is run on a Linux CentOS Dell Precision Workstation. The facility is located in RC1 South Building Rm 1301. It is directed by Dr. Mair Churchill (Department of Pharmacology), and is managed by John Hardin (Department of Biochemistry and Molecular Genetics).

Dr. Mair Churchill
Department of Pharmacology
CU Anschutz Medical Campus
12801 E. 17th Avenue, Mail Stop 8303
Aurora, CO 80045
Phone: 303-724-3670
Fax: 303-724-3663

Dr. Jeffrey Kieft
Department of Biochemistry and Molecular Genetics
CU Anschutz Medical Campus

12801 E. 17th Avenue, Mail Stop 8101
Aurora, CO 80045
Phone: 303-724-3257
Fax: 303-724-3215

Dr. Rui Zhao
Assistant Professor
Department of Biochemistry and Molecular Genetics
CU Anschutz Medical Campus
12801 E. 17th Avenue, Mail Stop 8101
Aurora, CO 80045
Phone: 303-724-3269
Fax: 303-724-3215

Dr. John Hardin
Research Associate, Manager of the X-ray Core Facility
Department of Biochemistry and Molecular Genetics
12801 E. 17th Avenue, Mail Stop 8101
Aurora, CO 80045
Phone: 303-724-3330



Safety Protocols

Available Software

    • hkl (denzo and scalepack): Data processing. Current version 1.96.6.
    • d*trek: Data processing. Current version DTREK72.
    • Chooch: A program for deriving anomalous scattering factors from X-ray fluorescence spectra.
    • CCP4: everything in crystallgoraphy except for data processing. Current version 4.1.
    • Epmr: A molecular replacement program
    • Replace: Another molecular replacement program
    • Shelx: Structural determination and refinement for small molecule. Also useful in finding heavy atom positions as well as refinement of high resolution protein structures. Current version SHELX-97.
    • Solve and Resolve: MIR/MAD structure determination and solvent flattening. Current version 2.01.
    • CNS: structure determination and refinement. Current version 1.1.
    • O: model building. Current version 8.0.
    • Grasp: Graphical Representation and Analysis of Structural Properties
    • Molscript and Bobscript: Graphical display of molecular 3D structures and electron densities.
    • Ribbons: Graphical representation of molecular 3D structures.

The primary users of the X-ray facility include Drs. Mair Churchill (Pharmacology), Elan Eisenmesser (Biochemistry and Molecular Genetics), Jeffrey Kieft (Biochemistry and Molecular Genetics), David Jones (Pharmacology), Tanya Kutateladze (Pharmacology), and Rui Zhao (Biochemistry and Molecular Genetics). In addition, these primary users collaborate with Richard Davis (Biochemistry and Molecular Genetics), Michael Holers (Immunology), Bob Garcia (Pediatrics), and Heide Ford (Obstetrics & Gynecology) in a variety of research areas. Some recent publications by these users are listed below.

Churchill ME, Klass J, Zoetewey DL. Structural analysis of HMGD-DNA complexes reveals influence of intercalation on sequence selectivity and DNA bending. J Mol Biol 403(1):88-102, 2010 [PMC2962916]

Roy S, Musselman CA, Kachirskaia I, Hayashi R, Glass KC, Nix JC, Gozani O, Appella E, Kutateladze TG. Structural insight into p53 recognition by the 53BP1 tandem Tudor domain. J Mol Biol 398(4):489-496, 2010.

Hammond JA, Rambo RP, Filbin ME, Kieft JS. Comparison and functional implications of the 3D architectures of viral tRNA-like structures. RNA 15(2):294-307, 2009.

Liu W, Zhao R, McFarland C, Kieft J, Niedzwiecka A, Jankowska-Anyszka M, Stepinski J, Darzynkiewicz E, Jones DN, Davis RE. Structural insights into parasite eIF4E binding specificity for m7G and m2,2,7G mRNA caps. J Biol Chem 284(45):31336-31349, 2009.

Gangelhoff TA, Mungalachetty PS, Nix JC, Churchill ME. Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A. Nucleic Acids Res 37(10):3153-3164, 2009 [PMC2691818]

Kieft JS. Comparing the three-dimensional structures of Dicistroviridae IGR IRES RNAs with other viral RNA structures. Virus Res 139(2):148-156, 2009 [PMC2673954]

Zhang L, Xu T, Maeder C, Bud LO, Shanks J, Nix J, Guthrie C, Pleiss JA, Zhao R. Structural evidence for consecutive Hel308-like modules in the spliceosomal ATPase Brr2. Nat Struct Mol Biol 16(7):731-739, 2009 [PMC2743687]

Champagne KS, Saksouk N, Pena PV, Johnson K, Ullah M, Yang XJ, Cote J, Kutateladze TG. The crystal structure of the ING5 PHD finger in complex with an H3K4me3 histone peptide. Proteins 72(4):1371-1376, 2008 [PMC2756976]

Laughlin, J.D., Ha T-S, Jones, D.N.M. and Smith, D.P. Activation of Pheromone-Sensitive Neurons is Mediated by Conformational Activation of a Pheromone-Binding Protein, Cell (2008) 133(7):1255-65.

Pfingsten JS, Constantino DA, Kieft JS. Structural basis for ribosome recruitment and manipulation by a viral IRES RNA. Science 314(5804):1450-1454, 2006

Chen Z, Zang J, Whetstine J, Hong X, Davrazou F, Kutateladze TG, Simpson M, Mao Q, Pan CH, Dai S, Hagman J, Hansen K, Shi Y, Zhang G. Structural insights into histone demethylation by JMJD2 family members. Cell 125(4):691-702, 2006

Shi X, Hong T, Walter KL, Ewalt M, Michishita E, Hung T, Carney D, Pena P, Lan F, Kaadige MR, Lacoste N, Cayrou C, Davrazou F, Saha A, Cairns BR, Ayer DE, Kutateladze TG, Shi Y, Cote J, Chua KF, Gozani O. ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression. Nature 442(7098):96-99, 2006

English CM, Adkins MW, Carson JJ, Churchill ME, Tyler JK. Structural basis for the histone chaperone activity of asf1. Cell 127(3):495-508, 2006

Pena PV, Davrazou F, Shi X, Walter KL, Verkhusha VV, Gozani O, Zhao R, Kutateladze TG. Molecular mechanism of histone H3K4me3 recognition by plant homeodomain of ING2. Nature 442(7098):100-103, 2006

© The Regents of the University of Colorado, a body corporate. All rights reserved.

Accredited by the Higher Learning Commission. All trademarks are registered property of the University. Used by permission only.