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X-ray Crystallography Core Facility Bookmark and Share

X-ray Crystallography Core Facility

The X-ray Crystallography Core Facility is one of the Shared Resources facilities at Beckman Research Institute of City of Hope.

The objectives of the facility are:
  1. Provide structural and biophysical information to understand mechanisms of biological systems at the atomic level
  2. Validate binding sites of lead compounds of therapeutic interest
  3. Facilitate lead discovery through co-crystallization of therapeutic targets and small molecule libraries

Services provided include:
  • Protein Expression and Purification
  • Biophysical Characterization of macromolecules and small molecules
  • Crystallization
  • Diffraction quality
  • Data collections
  • Structure determination
 
 
Research reported in this publication includes work performed in the X-ray Crystallography Core supported by the National Cancer Institute of the National Institutes of Health under award number P30CA33572. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

Assessment of authorship will be determined by the level of intellectual input, assay design and data analysis provided by Core leadership and staff members for each project individually based on NIH authorship guidelines.

Services

The X-ray crystallography Core provides a state-of-the-art facility for the generation of crystals and structure determination of macromolecules including proteins, DNA, RNA, and complexes between macromolecules and their ligands.  To complement structural data, the core provides state-of-the-art instrumentation to measure the affinities and kinetics of macromolecules with ligands and/or other macromolecules.  Finally, the core has assembled a 1250 member, fragment library to screen for potential lead compounds through differential scanning fluorimetry, SPR, ITC and diffraction methods.

Sample Analysis and Preparation

Consultation and in silico analysis
• Protein expression and purification (bacteria, insect or mammalian cell expression/ affinity or tag-less purification)
• Domain structure, including disorder and secondary structure prediction

Physical Analysis

• Native and SDS PAGE
• Limited Proteolysis and characterization by SDS-PAGE
• Size Exclusion Chromatography (analytical and preparative grade)
• Sedimentation Equilibrium analysis by Analytical Ultracentrifugation (AUC)
• Sedimentation Velocity analysis by AUC
• Surface Plasmon Resonance (SPR)
• Circular Dichroism (CD) Spectroscopy
• Isothermal Titration Calorimetry (ITC)
• Kinetic Exclusion Assay (KinExA)
• Differential Scanning Fluorimetry (DSF)

Crystallization

1. Set up crystallization trials at 4 ºC and/or 20 ºC.
a. Initial trials (e.g., appropriate concentrations)
b .Full scale trials (4 different 96 well factorials at 3 protein concentrations and 2 temperatures)

2. Optimization – additive screens, factorial overlays, macro and micro seeding

3. Automated imaging available for4 ºC and 20 ºC )

Diffraction quality

1. Test diffraction quality (loop and capillary mounting available)

2. Test/screen cryo-conditions

Data collection

1. Collect, reduce and merge data. Generate table of statistics
2. MAD/SAD phasing – help design, collect, reduce and merge MAD data
3. Generate table of statistics including anomalous dispersion differences

Structure Determination

1. Solve structure by Molecular Replacement
2. Solve structure by MAD/SAD phasing
3. Refine structure
4. Produce relevant statistics (e.g., R and Rfree, RMS deviations)
5. Structural analysis (superpositions, electrostatics, etc)
6. Deposit Structure at PDB
 

Equipment

The facility houses a Mosquito Crystallization Robot, a Formulatrix imaging robot (with Automated Crystal Screening at 4 ºC and 20 ºC), a Rigaku Micromax 007 with an R-AxisIV++, and an Oxford cryojet and relevant software and computational hardware for structure determination.
 
The facility also houses a Beckman XLI analytical ultracentrifuge and a GE Health Phast Gel system for the characterization of macromolecular properties.
 
Mosquito Crystallization Robot
The mosquito crystallization robot permits hanging drop, sitting drop, and batch methods in a 96 well format using minimal amounts of protein (~18 microL/trail). A number of commercial crystallization screens are available (Qiagen, Hampton Research, Jena).
   
Formulatrix Automated Visualization of Crystallization Trials
The core houses two Formulatrix imaging robots for visualization at 4 ºC and 20 ºC. Users can quickly browse images, score potential hits and follow crystal growth in time.
   
Rigaku X-ray Diffractometer
Micromax 007 HF, R-axis V++, and Oxford cryojets allow full structure determination.
 
 
Beckman XL-I Proteomelab
The Beckman Analytical ultracentrifuge affords accurate measurement of hydrodynamic properties, including the association constant of macromolecular complexes, as well as small molecule-macromolecular interactions.   It is also useful for formulation of biologics.
   
Waters NanoITC
Isothermal Titaction Calorimetry measures the transfers of thermal energy upon ligand binding.    Rom these measurements, one directly observes the enthalpy and measures the association constant of the interaction.  This in turn affords a measure of the entropy involved in an interaction.  These values provide important information about the nature of an interaction and are useful for drug design efforts.
   
Biacore T100 SPR
The GE Healthsciences Biacore provides kinetic and thermodynamic information for macromolecular interactions (protein-protein, DNA-protein, etc.), ligand-protein interactions, and fragments.
   
Jasco 815 Circular Dichroism
The Jasco 825 CD with fluorescence detection provides information vis-à-vis secondary structure.  Combined with a Peltier thermal control, this instrument is useful for determining melting temperatures and how point mutations affect protein stability.  In addition, the fluorescence detection can be used to determine the affinity protein-protein/protein-DNA interactions, how potential therapeutics affect such interactions, etc.
   
Sapidyne Kinexa 3200
The Sapidyne Kinexa determines binding constants and kinetics of an interaction by measuring the free ligand available (as opposed to SPR which measures the complex).  This allows the Kinexa to measure much tighter affinities (down to 10 femtomolar).
 
 
 
 
 
 
 

Abstract for Grants

The X-ray core at Beckman Research Institute of City of Hope is a state-of-the-art crystallization and X-ray facility for basic and translational science.  To facilitate investigators, the core also provides protein expression and purification as well as numerous biophysical methods to characterize stability, oligomerizaiton, and kinetic and thermodynamic properties.This facility houses a Mosquito Crystallization robot that uses 50 to 100 nL volumes and permits three different crystallization formats; hanging drop, sitting drops or batch methods under oil. The facility has multiple commercial crystallization factorials (e.g., Hampton, Jena, Nextal), To follow crystallization trials, two Formulatrix Imaging Robots at different temperatures are used that automatically image each drop, according to a preset schedule (e.g., nightly). This allows follow-up of crystallization trends at two temperatures and produces a visual record for analysis. A Rigaku 007HF generator,  R-axis IV++ imager and an Oxford cryojet (for data collection at 100 K) is used for in-house diffraction studies and access to SSRL and other synchrotrons is available The facility has all the software and computational hardware necessary to determine structures of macromolecular complexes.
 
In addition, our core facility has capabilities to express and purify large quantities of high quality protein (1 to 100 mg +) using a variety of expression systems (bacteria, insect and mammalian cells). Biophysical characterization of macromolecules and small molecules can be carried out using SPR, ITC, AUC, analytical SEC, KinExa and CD and fluorescent spectroscopy.
 

Pricing

Prices and availability vary. Please contact us or visit our site on iLab Solutions for current information.

 

 

FAQ

How pure does my sample have to be? For both biophysical characterization and crystallography experiments, the highest level of purity obtainable for your macromolecule is crucial to obtaining high quality data. How pure is pure enough?

This is difficult to answer, but if you can provide material that is 95% or higher purity as estimated by assays such as gel electrophoresis, mass spec. analysis or other analytical chromatography technique, this will give the best chance of success.

What buffer should I use?

If you are providing us with your macromolecule, use a buffer, which contains the minimal number of components (buffers, stabilizing agents, salts) and lowest concentrations of those components that stabilize your molecule. Every marcomolecule is different and therefore may require different buffers. 10-20 mM TRIS/HEPES/MES etc. buffering agent with 50-100 mM NaCl is a good place to start. Your sample may require additional component such as Mg2+ for oligonucleotide samples, glycerol or ethylene glycol for samples that aggregate easily, reducing agents such as DTT or TCEP etc. Small molecule compounds should be provided as a lyophilized powder when possible and as a high concentration liquid when necessary. If DMSO or DMF are in your small molecule solution, we need to know how much.
 
Typical/Example buffers by assay:
 
  • Crystallography- 10 mM Tris pH 8.0, 25-100 mM NaCl
  • SPR- 50 mM Hepes pH 7.4, 150 mM NaCl, 1 mM EDTA, 0.05% Tween/ or PBST (avoid components with high refractive indices and high  viscocities when possible such as DMSO, sucrose, glycerol etc.)
  • CD spectroscopy- low concentrations of UV-Vis inactive buffering agents. Avoid chloride, citrates, MOPS, immidazole and DTT as these  components absorb in the visible and/or UV region.  Phosphate and Tris buffers are common (do not pH with HCl). De-gas all buffers prior to  analysis.
  • AUC- PBS is commonly used. Ensure that all biomacromolecules are dialyzed into the same batch of buffer. Provide the Core staff with a  small volume of your dialysis buffer for dilutions and reference channels.
  • ITC –PBS or Tris are commonly used depending on the type of interaction that you are studying (proton dependent or independent).  Dialyze all samples into the same batch of buffer and provide a sample of that buffer to the core staff along with your sample. Degas all  buffers and samples immediately prior to analysis.
  • KinExA- PBS is typically used as a buffer. BSA will be added to samples prior to analysis.
  • DSF- flexible buffers, but HEPES is typical.

How much sample do I need to provide?

This question will require a consultation with a Core staff member to determine. The answer depends on your assay and your biomacromolecule. When you meet with a core staff member to discuss the experimental design, be sure to mention if you have a reagent which is a limiting factor. Perhaps the assay can be designed to minimize the usage of your more precious reagent. Very generally speaking, 10-20 mg for crystallography, 1-10 mg for ITS/DSF/CD/KinExA and 100 ug-1mg for SPR.

What information do I need to provide the Core when I drop off my samples?

Please label your tubes legibly and include important information such as a) name of sample, b) concentration of sample and c) buffer components and concentrations. It is also helpful if you can provide us with as much information as you have with your macromolecule such as any know information about purity, how stable it is in different pH salt or temperature conditions, how high it can tolerate being concentrated etc. The more information you can provide, the better. Also let us know how we should store the protein prior to and during experimentation.

How should I deliver my macromolecule?

If you are delivering your protein to us personally, please bring it on ice if it is in a thawed state already or bring it frozen on dry ice if it was previously frozen or a lyophilized powder. If you are shipping us your material, email us in advance to ensure that we have someone here to receive it. Ship it overnight either on ice or frozen on dry ice.

Can I be trained on the instrumentation?

For most of our instrumentation, the answer is yes. If you are interested in running your own samples and learning these techniques, please contact a core staff member and arrange for a time to meet and assess the amount of training that you will likely require based on previous experience. Once training and familiarity is established you will be an approved user, with access to the instrumentation at your convenience. However, if you are not interested or don’t have the time to put into training on each instrument, leave the work to us. We are happy to characterize your samples on your behalf.

How far in advance do I need to sign up for instrument time?

For instrumentation that requires gas (X-ray diffraction and CD spectroscopy), please contact a core staff member at least 2 days in advance so that we have time to order new gas tanks if necessary. For all other instrumentation review the instruments availability using our iLab reservations tab and contact a core staff member to reserve time on your behalf.

What else do I need to bring with me?

The core provides you access to pipets, tips, tubes etc. along with most of the items you would need for a typical experiment on an instrument (examples include plates for crystallography experiments, quartz cuvettes for CD, tubes for SPR etc.). If you have an uncommon protocol or special needs/reagents, please plan to bring those items with you or contact a core staff member to ask if we have those items in stock.

Contact Us

John C. Williams, Ph.D., Director
jcwilliams@coh.org
Flower Building, Room 148
Phone:  626-256-HOPE (4673), ext. 60227
 
Kendra N. Avery, Ph.D. Staff Scientist
kavery@coh.org
Flower Building, Room 137C
Phone 626-256-HOPE (4673), ext. 65986
 
Krzysztof Bzymek, Ph.D. Staff Scientist
kbzymek@coh.org
Flower Building, Room 137C
Phone 626-256-HOPE (4673), ext. 65986
 

X-ray Crystallography Core Facility

X-ray Crystallography Core Facility

The X-ray Crystallography Core Facility is one of the Shared Resources facilities at Beckman Research Institute of City of Hope.

The objectives of the facility are:
  1. Provide structural and biophysical information to understand mechanisms of biological systems at the atomic level
  2. Validate binding sites of lead compounds of therapeutic interest
  3. Facilitate lead discovery through co-crystallization of therapeutic targets and small molecule libraries

Services provided include:
  • Protein Expression and Purification
  • Biophysical Characterization of macromolecules and small molecules
  • Crystallization
  • Diffraction quality
  • Data collections
  • Structure determination
 
 
Research reported in this publication includes work performed in the X-ray Crystallography Core supported by the National Cancer Institute of the National Institutes of Health under award number P30CA33572. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health.

Assessment of authorship will be determined by the level of intellectual input, assay design and data analysis provided by Core leadership and staff members for each project individually based on NIH authorship guidelines.

Services

Services

The X-ray crystallography Core provides a state-of-the-art facility for the generation of crystals and structure determination of macromolecules including proteins, DNA, RNA, and complexes between macromolecules and their ligands.  To complement structural data, the core provides state-of-the-art instrumentation to measure the affinities and kinetics of macromolecules with ligands and/or other macromolecules.  Finally, the core has assembled a 1250 member, fragment library to screen for potential lead compounds through differential scanning fluorimetry, SPR, ITC and diffraction methods.

Sample Analysis and Preparation

Consultation and in silico analysis
• Protein expression and purification (bacteria, insect or mammalian cell expression/ affinity or tag-less purification)
• Domain structure, including disorder and secondary structure prediction

Physical Analysis

• Native and SDS PAGE
• Limited Proteolysis and characterization by SDS-PAGE
• Size Exclusion Chromatography (analytical and preparative grade)
• Sedimentation Equilibrium analysis by Analytical Ultracentrifugation (AUC)
• Sedimentation Velocity analysis by AUC
• Surface Plasmon Resonance (SPR)
• Circular Dichroism (CD) Spectroscopy
• Isothermal Titration Calorimetry (ITC)
• Kinetic Exclusion Assay (KinExA)
• Differential Scanning Fluorimetry (DSF)

Crystallization

1. Set up crystallization trials at 4 ºC and/or 20 ºC.
a. Initial trials (e.g., appropriate concentrations)
b .Full scale trials (4 different 96 well factorials at 3 protein concentrations and 2 temperatures)

2. Optimization – additive screens, factorial overlays, macro and micro seeding

3. Automated imaging available for4 ºC and 20 ºC )

Diffraction quality

1. Test diffraction quality (loop and capillary mounting available)

2. Test/screen cryo-conditions

Data collection

1. Collect, reduce and merge data. Generate table of statistics
2. MAD/SAD phasing – help design, collect, reduce and merge MAD data
3. Generate table of statistics including anomalous dispersion differences

Structure Determination

1. Solve structure by Molecular Replacement
2. Solve structure by MAD/SAD phasing
3. Refine structure
4. Produce relevant statistics (e.g., R and Rfree, RMS deviations)
5. Structural analysis (superpositions, electrostatics, etc)
6. Deposit Structure at PDB
 

Equipment

Equipment

The facility houses a Mosquito Crystallization Robot, a Formulatrix imaging robot (with Automated Crystal Screening at 4 ºC and 20 ºC), a Rigaku Micromax 007 with an R-AxisIV++, and an Oxford cryojet and relevant software and computational hardware for structure determination.
 
The facility also houses a Beckman XLI analytical ultracentrifuge and a GE Health Phast Gel system for the characterization of macromolecular properties.
 
Mosquito Crystallization Robot
The mosquito crystallization robot permits hanging drop, sitting drop, and batch methods in a 96 well format using minimal amounts of protein (~18 microL/trail). A number of commercial crystallization screens are available (Qiagen, Hampton Research, Jena).
   
Formulatrix Automated Visualization of Crystallization Trials
The core houses two Formulatrix imaging robots for visualization at 4 ºC and 20 ºC. Users can quickly browse images, score potential hits and follow crystal growth in time.
   
Rigaku X-ray Diffractometer
Micromax 007 HF, R-axis V++, and Oxford cryojets allow full structure determination.
 
 
Beckman XL-I Proteomelab
The Beckman Analytical ultracentrifuge affords accurate measurement of hydrodynamic properties, including the association constant of macromolecular complexes, as well as small molecule-macromolecular interactions.   It is also useful for formulation of biologics.
   
Waters NanoITC
Isothermal Titaction Calorimetry measures the transfers of thermal energy upon ligand binding.    Rom these measurements, one directly observes the enthalpy and measures the association constant of the interaction.  This in turn affords a measure of the entropy involved in an interaction.  These values provide important information about the nature of an interaction and are useful for drug design efforts.
   
Biacore T100 SPR
The GE Healthsciences Biacore provides kinetic and thermodynamic information for macromolecular interactions (protein-protein, DNA-protein, etc.), ligand-protein interactions, and fragments.
   
Jasco 815 Circular Dichroism
The Jasco 825 CD with fluorescence detection provides information vis-à-vis secondary structure.  Combined with a Peltier thermal control, this instrument is useful for determining melting temperatures and how point mutations affect protein stability.  In addition, the fluorescence detection can be used to determine the affinity protein-protein/protein-DNA interactions, how potential therapeutics affect such interactions, etc.
   
Sapidyne Kinexa 3200
The Sapidyne Kinexa determines binding constants and kinetics of an interaction by measuring the free ligand available (as opposed to SPR which measures the complex).  This allows the Kinexa to measure much tighter affinities (down to 10 femtomolar).
 
 
 
 
 
 
 

Abstract for Grants

Abstract for Grants

The X-ray core at Beckman Research Institute of City of Hope is a state-of-the-art crystallization and X-ray facility for basic and translational science.  To facilitate investigators, the core also provides protein expression and purification as well as numerous biophysical methods to characterize stability, oligomerizaiton, and kinetic and thermodynamic properties.This facility houses a Mosquito Crystallization robot that uses 50 to 100 nL volumes and permits three different crystallization formats; hanging drop, sitting drops or batch methods under oil. The facility has multiple commercial crystallization factorials (e.g., Hampton, Jena, Nextal), To follow crystallization trials, two Formulatrix Imaging Robots at different temperatures are used that automatically image each drop, according to a preset schedule (e.g., nightly). This allows follow-up of crystallization trends at two temperatures and produces a visual record for analysis. A Rigaku 007HF generator,  R-axis IV++ imager and an Oxford cryojet (for data collection at 100 K) is used for in-house diffraction studies and access to SSRL and other synchrotrons is available The facility has all the software and computational hardware necessary to determine structures of macromolecular complexes.
 
In addition, our core facility has capabilities to express and purify large quantities of high quality protein (1 to 100 mg +) using a variety of expression systems (bacteria, insect and mammalian cells). Biophysical characterization of macromolecules and small molecules can be carried out using SPR, ITC, AUC, analytical SEC, KinExa and CD and fluorescent spectroscopy.
 

Pricing

Pricing

Prices and availability vary. Please contact us or visit our site on iLab Solutions for current information.

 

 

FAQs

FAQ

How pure does my sample have to be? For both biophysical characterization and crystallography experiments, the highest level of purity obtainable for your macromolecule is crucial to obtaining high quality data. How pure is pure enough?

This is difficult to answer, but if you can provide material that is 95% or higher purity as estimated by assays such as gel electrophoresis, mass spec. analysis or other analytical chromatography technique, this will give the best chance of success.

What buffer should I use?

If you are providing us with your macromolecule, use a buffer, which contains the minimal number of components (buffers, stabilizing agents, salts) and lowest concentrations of those components that stabilize your molecule. Every marcomolecule is different and therefore may require different buffers. 10-20 mM TRIS/HEPES/MES etc. buffering agent with 50-100 mM NaCl is a good place to start. Your sample may require additional component such as Mg2+ for oligonucleotide samples, glycerol or ethylene glycol for samples that aggregate easily, reducing agents such as DTT or TCEP etc. Small molecule compounds should be provided as a lyophilized powder when possible and as a high concentration liquid when necessary. If DMSO or DMF are in your small molecule solution, we need to know how much.
 
Typical/Example buffers by assay:
 
  • Crystallography- 10 mM Tris pH 8.0, 25-100 mM NaCl
  • SPR- 50 mM Hepes pH 7.4, 150 mM NaCl, 1 mM EDTA, 0.05% Tween/ or PBST (avoid components with high refractive indices and high  viscocities when possible such as DMSO, sucrose, glycerol etc.)
  • CD spectroscopy- low concentrations of UV-Vis inactive buffering agents. Avoid chloride, citrates, MOPS, immidazole and DTT as these  components absorb in the visible and/or UV region.  Phosphate and Tris buffers are common (do not pH with HCl). De-gas all buffers prior to  analysis.
  • AUC- PBS is commonly used. Ensure that all biomacromolecules are dialyzed into the same batch of buffer. Provide the Core staff with a  small volume of your dialysis buffer for dilutions and reference channels.
  • ITC –PBS or Tris are commonly used depending on the type of interaction that you are studying (proton dependent or independent).  Dialyze all samples into the same batch of buffer and provide a sample of that buffer to the core staff along with your sample. Degas all  buffers and samples immediately prior to analysis.
  • KinExA- PBS is typically used as a buffer. BSA will be added to samples prior to analysis.
  • DSF- flexible buffers, but HEPES is typical.

How much sample do I need to provide?

This question will require a consultation with a Core staff member to determine. The answer depends on your assay and your biomacromolecule. When you meet with a core staff member to discuss the experimental design, be sure to mention if you have a reagent which is a limiting factor. Perhaps the assay can be designed to minimize the usage of your more precious reagent. Very generally speaking, 10-20 mg for crystallography, 1-10 mg for ITS/DSF/CD/KinExA and 100 ug-1mg for SPR.

What information do I need to provide the Core when I drop off my samples?

Please label your tubes legibly and include important information such as a) name of sample, b) concentration of sample and c) buffer components and concentrations. It is also helpful if you can provide us with as much information as you have with your macromolecule such as any know information about purity, how stable it is in different pH salt or temperature conditions, how high it can tolerate being concentrated etc. The more information you can provide, the better. Also let us know how we should store the protein prior to and during experimentation.

How should I deliver my macromolecule?

If you are delivering your protein to us personally, please bring it on ice if it is in a thawed state already or bring it frozen on dry ice if it was previously frozen or a lyophilized powder. If you are shipping us your material, email us in advance to ensure that we have someone here to receive it. Ship it overnight either on ice or frozen on dry ice.

Can I be trained on the instrumentation?

For most of our instrumentation, the answer is yes. If you are interested in running your own samples and learning these techniques, please contact a core staff member and arrange for a time to meet and assess the amount of training that you will likely require based on previous experience. Once training and familiarity is established you will be an approved user, with access to the instrumentation at your convenience. However, if you are not interested or don’t have the time to put into training on each instrument, leave the work to us. We are happy to characterize your samples on your behalf.

How far in advance do I need to sign up for instrument time?

For instrumentation that requires gas (X-ray diffraction and CD spectroscopy), please contact a core staff member at least 2 days in advance so that we have time to order new gas tanks if necessary. For all other instrumentation review the instruments availability using our iLab reservations tab and contact a core staff member to reserve time on your behalf.

What else do I need to bring with me?

The core provides you access to pipets, tips, tubes etc. along with most of the items you would need for a typical experiment on an instrument (examples include plates for crystallography experiments, quartz cuvettes for CD, tubes for SPR etc.). If you have an uncommon protocol or special needs/reagents, please plan to bring those items with you or contact a core staff member to ask if we have those items in stock.

Contact Us

Contact Us

John C. Williams, Ph.D., Director
jcwilliams@coh.org
Flower Building, Room 148
Phone:  626-256-HOPE (4673), ext. 60227
 
Kendra N. Avery, Ph.D. Staff Scientist
kavery@coh.org
Flower Building, Room 137C
Phone 626-256-HOPE (4673), ext. 65986
 
Krzysztof Bzymek, Ph.D. Staff Scientist
kbzymek@coh.org
Flower Building, Room 137C
Phone 626-256-HOPE (4673), ext. 65986
 
Research Shared Services

City of Hope embodies the spirit of scientific collaboration by sharing services and core facilities with colleagues here and around the world.
 

Recognized nationwide for its innovative biomedical research, City of Hope's Beckman Research Institute is home to some of the most tenacious and creative minds in science.
City of Hope is one of only 41 Comprehensive Cancer Centers in the country, the highest designation awarded by the National Cancer Institute to institutions that lead the way in cancer research, treatment, prevention and professional education.
Learn more about City of Hope's institutional distinctions, breakthrough innovations and collaborations.
Support Our Research
By giving to City of Hope, you support breakthrough discoveries in laboratory research that translate into lifesaving treatments for patients with cancer and other serious diseases.
 
 
 
 
Media Inquiries/Social Media

For media inquiries contact:

Dominique Grignetti
800-888-5323
dgrignetti@coh.org

 

For sponsorships inquiries please contact:

Stefanie Sprester
213-241-7160
ssprester@coh.org

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213-241-7112
cnassr@coh.org

 
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