Small-Angle X-ray Scattering (SAXS) Facility Back

The facility also houses the Small Angle X-ray Scattering (SAXS) System to decipher the physical and structural features of macromolecules in solution.

Small-Angle X-ray Scattering (SAXS) is a technique for probing size, shape, quarternary structure and complex formation of molecules in solution without crystallization. It helps in understanding structural parameters [radius of gyration (Rg), maximum Dimension (Dmax), partial-specific volume (Vp) etc], dynamics of molecules and also generation of low-resolution shapes of molecules.


The SAXS facility at CCMB is S3-MICRO Point-Focus system, Hecus X-ray systems, GmbH.


Experimental Setup:

  • Source power : 50 Watt

  • X-rays : Cu-Kα (λ=1.54 Å)

  • Beam Size at sample : 50 x 200 µm2

  • Photon flux : up to 2 x 108 photons/sec

  • Brilliance > 1010 (comaparable to that of a bending-magnet synchrotron SAXS beamlines)

  • Point focus at detector : monochromatic (Convergent beam <1 mrad)

  • Sample-detector distance : 300mm

  • Q-range : 0.003 to 0.6 Å-1 enables to cover a distance range of 2000 to 11 Å.

  • Pilatus 100k detector with a pixel size of 172*172 µm2.

  • SAXS Resolution range : 2000 Å to 30 Å.

SAXS Sample Requirement:

  • Sample quality recommended : monodisperse macromolecule sample with buffer 

  • (DLS,   Ultracentrifugation, gel analysis, etc.)
  • Concentration range : min. 1 mg/ml to max. 10 mg/ml
    [depends on the protein size; typically a concentration series (e.g. 1,2,3,5,10 mg/ml) has to be measured]

  • Buffer should contain minimum amount of additives.

  • Sample volume : 50-60 µl for a single SAXS measurement.

  • Temperature range : 10 ºC to 37 ºC.

  • Exposure time is 3600 s or 3000 s.


Scientist In-Charge 
Dr. Rajan Sankarayanayanan Ph.: 27192832

Technical In-Charge 
Ms. R. Rukmini Ph: 27192953 (R-100, R & D); 27192835 (Lab, Main Building)
Mr. K. Mallesham Ph:27192921

Instrumentation In-Charge 
Mr. Venkatnarayana Ph : 27192591

SAXS-Lab [New R & D Structural Biology Facility] : Room:107 Ph.:27192919


  1. Thakur AK, Srivastava AK, Srinivas V, Chary KV, & Rao CM (2011) Copper alters aggregation behavior of prion protein and induces novel interactions between its N- and C-terminal regions. J Biol Chem 286(44):38533-38545.

  2. Prabhu S, Srinivas V, Ramakrishna T, Raman B, & Rao Ch M (2011) Inhibition of Cu2+-mediated generation of reactive oxygen species by the small heat shock protein alphaB-crystallin: the relative contributions of the N- and C-terminal domains. Free Radic Biol Med 51(3):755-762.

  3. Arush Chhabra, Asfarul Haque S., Ravi Kant Pal, Aneesh Goyal, Rajkishore Rai, Seema Joshi, Santosh Panjikar, Santosh Pasha, Rajan Sankaranarayanan and Rajesh S. Gokhale (2012) Nonprocessive [2+2]e- Offloading Reductase Domains from Mycobacterial Non-ribosomal Peptide Synthetases Proc. Natl. Acad. Sci. (USA) 109 (15); 5681-5686.

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