.
Category
- Spectroscopy and Spectrometry » Mass Spectrometry
Booking Details
Facility Management Team and Location
Facility Features, Working Principle and Specifications
Facility Description
autoflex maX™ MALDI TOF/TOF System:
MALDI-Time-Of-Flight Mass Spectrometer for accurate mass determination and structure identification of bio-molecules.
Includes MALDI Perpetual™ ion source with self-cleaning device, extended pulsed ion extraction PAN™ mass range focusing; Bruker smart beam™-II laser technology for versatile applications with different sample preparation techniques; TOF analyser for linear and reflection measurements in positive/negative ion mode with integrated FlashDetector™ systems; MS/MS capability based on LIFT™ TOF/TOF technology; high-energy CID (Collision-Induced Dissociation) accessory Data System with 10 bit 5 Gs/s digitizer, WIN10 Operating-System, >=24| Widescreen-LCD-Display and Compass™ for Flex software package for MS control, data acquisition and processing
Features:
BioTools software allows the identification and detailed characterization of proteins and peptides using various types of mass spectra.
This includes database search of single spectra and combined MS and MS/MS datasets, the import of search results and further detection of modifications and mutations.
The RapiDeNovo module provides extensive de-novo sequencing capabilities.
BioTools also supports various top-down sequencing spectra types for intact protein characterization and enables the annotation and database search of these data.
PolyTools™ 2.0 is a program for the interpretation of MALDI mass spectra of polymers. It accepts peak lists and automatically detect the repeat unit, cation and end groups upon loading of the lists. It also calculates characteristic parameters of the chain length distribution like |molecular weight average|, |polydispersity| or |degree of polymerization|. It displays the results in tabular and graphical representation and can export both for further use in other programs. Kendrick Mass Defect (KMD) analysis of the data is possible as well and a variety of KMD analysis types/plots is available (KMD, KMD-RNKM, RKM and RKM-RNKM).
smartbeam II (DPSS) Used in autoflex max MALDI TOF TOF. The smartbeam I components (modulator, focus lens, pin hole) are inside the laser housing.
Wave length : 355 nm (diode pumped solid state laser)
Pulse duration : > 3ns
Pulse energy : < 100µJ
Repetition rate : 2000 Hz
Beam diameter: smartbeam pattern
Divergence : smartbeam pattern
Lifetime : 3.5 x109 shoots
Power supply : 100 - 240 V
Instructions for Registration, Sample Preparation, User Instructions and Precautionary Measures
- External Users can come in-person or send your samples along with a letter from the Head / Guide on your College/Institute /Industry Original Letter Head for registration stating that the analysis is for research purpose to qualify for academic concession.
- The analytical data / spectra are provided only for research / development purposes. These cannot be used as certificates in legal disputes.
- Service charges are payable at prevailing rates.
- Samples, letter and payment should be sent in the same cover only. If Samples are received without covering letter the samples will be sent back to the user without any further intimation/notice. Separate Sample should be sent for different analysis.
- Samples are not analysed till Payment is received.
- Please send the samples in quantity as mentioned. Samples are not recovered, unless a special request is made.
- Radio -active material should be clearly mentioned and handed over personally.
- Unstable and explosive compounds are not accepted for analysis.
- Kindly fill separate sample submission forms for different sample type with complete
information as requested in the sample submission form. - Also please fill the check list for the tolerance for common buffer compounds / solvents
used during sample preparation / processing attached with this form (pg-3). - SDS-PAGE image for proteins is mandatory and for other sample types mass information of
any other suitable data will be accepted. - Zip-tipping of samples is must for all peptide analysis and also for proteins wherever
required (will be confirmed by the MALDI staff in charge)
INSTRUCTIONS FOR SAMPLE PREPARATION :
• Experiments should be discussed with the facility in-charge before appointment.
• Purity of samples is extremely important for generating good data.
• Protein concentrations should be measured accurately before starting the experiment.
• The molecular weight (SDS IMAGE copy mandatory)as well as the pI of the proteins should
be known before analysis.
• Zip-tipping of samples must for all peptide analysis and also for proteins wherever required (will be confirmed by the MALDI staff in charge).
• Appointments will be provided as per que and the user will be informed about the same.
• Kindly perform literature review on similar work and accumulate as much information as
possible for good quality data.
• Any query regarding your MALDI experiment can be emailed on rajeshg@chem.iitb.ac.in
Whenever the prepared samples are used in the publications appropriate acknowledgement of usage of Chemistry, IIT Bombay MALDI facility must be mentioned. The details should be forwarded to rajeshg@chem.iitb.ac.in
General Instructions for MALDI TOF/TOF Users:
Mass spectrometry is highly sensitive to various contaminants, such as PEG (poly ethylene glycol), keratin and various salts. In order to reduce PEG and keratin in the sample it is recommended to use powder free nitryl gloves. Please supply the sample in a low-salt buffer (less than 10 mM).
- Use fresh solutions. All solvents should be pure as possible. HPLC grade is recommended.
- Avoid volatile solvents! Several of these solvents are common in protein chemistry: glycerol, polyethylene glycol,b-mercaptoethanol,triton-X-100,DMSO,DMF,etc.
- Scalpel, pipette tips and tubes should be clean. Use original Eppendorf tubes. Since the solvents can leach the plastics and polymer contamination can occur.
- Sequencing grade trypsin is recommended
It is recommended to use the Coomassie / silver staining Standard protocol.
Levels of buffers and detergents which exceed the following limits will probably cause noticeable degradation of the spectrum
Phosphate Buffer >50 mM
Ammonium Bicarbonate > 30 mM
Tris Buffer >100 mM
Guanidine >1M
Detergent(e.g. Trition-X) 0.1%
SDS 0.01%
Alkali metal salts >1M
Glycerol >1%
Sodium azide >1 mM
Charges for Analytical Services in Different Categories
Charges for External Users: (a) Basic charges + (b) GST*
(a) Basic charges:
Type of samples |
Type of analysis |
IITB Users ( in ₹ ) | Academic institutes ( in ₹ ) | National R &D lab`s (in ₹ ) | Industries / Non Govt. Agencies (in ₹ ) |
| Small Molecules | MS analysis | 50 | 100 | 500 | 1000 |
| Intact Protein | MS analysis | 200 | 400 | 1000 | 2000 |
| Oligonucleotides | MS analysis | 200 | 400 | 1000 | 2000 |
| Peptide mass fingerprinting | MS analysis | 200 | 400 | 1000 | 2000 |
MS/MS analysis | 300 | 600
| 1500 | 3000 |
(b)GST*(rate as on 1.8.2017):
1) If the recipient of the report is from Maharashtra: 9% SGST and 9% CGST 2) If the recipient of the report is from outside Maharashtra: 18% IGST
- Payment Terms: 100% Advance
Payment Bank Details for Electronic Transfer:
Account Name: Indian Institute of Technology
Bombay Bank Name: State Bank of India, IIT Powai Branch, Mumbai-400076, India
Account Number: 10725729173
IFSC Code: SBIN0001109
MICR Code: 400002034 Branch Code: 1109
SWIFT Code: SBININBB519
Bank Contact Number: +91-22-2572-1103
Applications
- Molecular weight determination of intact proteins
- Partial protein sequencing
- Protein identification
- N-terminal sequencing
- Small molecule detection
- Nucleic acid and oligo nucleotide detection
- Polymer detection
Sample Details
NO