Please download Sample Submission Form and fill it out electronically using Adobe Acrobat. Submitter and sample information parts must be filled out completely. Print out the form and attach your labeled sample at the top-right corner of the form (within “attach your sample here” box). We ask internal/external users to deliver samples with completed submission forms to:
CUNY Advanced Science Research Center
Mass Spectrometry Core Facility, SBI 3rd floor
85 Saint Nicholas Terrace
New York, NY 10031
Fill out the CUNY ASRC Structural Biology Initiative Facilities New User Form online. Information required:
PI and account information
General Information on Sample Preparation
Water, methanol, acetonitrile, tetrahydrofuran, propanol, ethanol, toluene, dichloromethane, nitromethane are MALDI-MS and ESI-MS compatible solvents, whereas non-volatile solvents as e.g. dimethilformamide or dimethyl sulfoxide are not (though tolerable in small amounts) – so please avoid using them. Protein samples for ESI or MALDI MS should be prepared using ultra-pure water (MilliQ 18MΩ cm, or LC-MS grade bottled water). Common buffers (Tris-HCl, HEPES, phosphate buffers, NaCl) are also not compatible with direct infusion ESI-MS analysis as they cause suppression of ESI/MALDI signal and/or extensive adduct formation. Appropriate volatile buffers for protein intact mass analysis include formic acid (up to 1%), acetic acid (up to 5%), ammonium acetate (up to 150mM), ammonium formate (up to 10mM), ammonium bicarbonate (up to 20 mM) and ammonium hydroxide.
Measurement accuracy expected at Low-Res is about +-0.05 Da for ESI-MS methods. Mass accuracy at High-Res is better than 5ppm and needed in general for publication purposes.
For further information, please contact ASRC Mass Spectrometry Core Facility Manager Rinat Abzalimov at Rinat.Abzalimov(at)asrc.cuny.edu or via telephone at 212-413-3236.