X-ray Scattering (SAXS) Facility
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.
Source power : 50 Watt
Cu-Kα (λ=1.54 Å)
Beam Size at sample : 50 x 200
Photon flux : up to 2 x
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
Pilatus 100k detector with a pixel size of 172*172
SAXS Resolution range : 2000
to 30 Å.
SAXS Sample Requirement:
(DLS, Ultracentrifugation, gel analysis, etc.)
Sample quality recommended : monodisperse macromolecule sample with buffer
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.
Dr. Rajan Sankarayanayanan firstname.lastname@example.org Ph.: 27192832
Ms. R. Rukmini email@example.com Ph: 27192953 (R-100, R & D); 27192835 (Lab, Main Building)
Mr. K. Mallesham firstname.lastname@example.org Ph:27192921
Mr. R. E. C. Johnson email@example.com Ph: 27192581
Mr. Venkatnarayana firstname.lastname@example.org Ph : 27192591
SAXS-Lab [New R & D Structural Biology Facility] : Room:107 Ph.:27192919
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.
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.
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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(Last Updated on 15/07/2013)