Instrument name: PETRA III EMBL P12 / City: Hamburg / 国: Germany / Type of source: X-ray synchrotronSynchrotron / Wavelength: 0.123982 Å / Dist. spec. to detc.: 3 mm
Detector
Name: Pilatus 6M
Scan
Title: Bovine serum albumin, purified dimer - SEC-SAXS coupled to multiangle laser and quasi-elastic light scattering (MALLS and QELS) Measurement date: Apr 5, 2019 / Storage temperature: 20 °C / Cell temperature: 20 °C / Exposure time: 1 sec. / Number of frames: 25 / Unit: 1/nm /
Min
Max
Q
0.1338
6.7984
Distance distribution function P(R)
Sofotware P(R): GNOM 5.0 / Number of points: 1684 /
Min
Max
Q
0.136558
4.78876
P(R) point
1
1684
R
0
13.2
Result
Type of curve: sec Comments: BSA dimer underwent pre-purification prior to SEC-SAXS using the following method. All procedures were performed at 4 oC. Protein powder (Sigma) consisting of BSA monomers, dimers, trimers ...Comments: BSA dimer underwent pre-purification prior to SEC-SAXS using the following method. All procedures were performed at 4 oC. Protein powder (Sigma) consisting of BSA monomers, dimers, trimers and higher MW species was made to approximately 25 mg/ml in 25 mM HEPES, 50 mM NaCl, 5 mM urea, 1% v/v glycerol, pH 7. Approximately 200 μl of sample were loaded onto a Superdex 200 Increase 10/300 column (GE Healthcare) equilibrated in the same buffer (flow rate = 0.4 ml/min). Fractionated aliquots corresponding to the minor dimer peak (estimated using UV A280 and UV A245 nm) were pooled and concentrated (30 kDa centrifuge spin filter) to a final concentration of 5 mg/ml (the concentration was determined from triplicate UV A280 measurements using an E0.1% of 0.646 (= 1 g/l) calculated from the amino acid sequence (ProtParam)). Approximately 50 μl aliquots were snap-frozen in liquid nitrogen then stored at -80oC prior to the SEC-SAXS analysis that was performed at room temperature in 50 mM HEPES, 150 mM NaCl, 2% v/v glycerol, pH 7. The Rg-correlation through the SEC-SAXS peak, the individual unsubtracted SEC-SAXS frames as well as the results from coupled MALLS and QELS analysis are included in the full entry zip archive. The quoted experimental molecular weight was determined using MALLS in combination with refractive-index (RI) measurements that were recorded from the same sample eluting from the column using a split-flow SEC-SAXS-light scattering configuration (Graewert et al., (2015) Sci. Reports. 5, 10734: doi: 10.1038/srep10734). The average hydrodynamic radius of the protein is 4.6 nm.
Experimental
Porod
MW
126 kDa
132 kDa
Volume
-
211 nm3
P(R)
Guinier
Guinier error
Forward scattering, I0
12430
12356
9
Radius of gyration, Rg
4.012 nm
3.95 nm
-
Min
Max
D
-
13.2
Guinier point
1
71
+
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