| MWexperimental | 100 | kDa |
| MWexpected | 101 | kDa |
| VPorod | 125 | nm3 |
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log I(s)
2.51×102
2.51×101
2.51×100
2.51×10-1
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s, nm-1
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Massively parallel, computationally guided design of a proenzyme.
Yachnin BJ, Azouz LR, White RE 3rd, Minetti CASA, Remeta DP, Tan VM, Drake JM, Khare SD, Proc Natl Acad Sci U S A 119(15):e2116097119 (2022) Europe PMCSASDLJ2 – Pro-CPG2-2 (pro-enzyme design 2 of circular permutant Carboxypeptidase G2-CP-N89-K177A) with Methotrexate
MethotrexatePro-Carboxypeptidase G2 (circular permutant CP-N89) K177A Design 2
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Fits and models
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Synchrotron SAXS
data from solutions of
Pro-CPG2-2 (pro-enzyme design 2 of circular permutant Carboxypeptidase G2-CP-N89-K177A) with Methotrexate
in
50 mM Tris, 100 mM NaCl, pH 7.4
were collected
on the
12.3.1 (SIBYLS) beam line
at the Advanced Light Source (ALS) storage ring
(Berkeley, CA, USA)
using a Pilatus3 X 2M detector
(I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle).
Solute concentrations ranging between 2 and 10 mg/ml were measured
at 10°C.
32 successive
0.300 second frames were collected.
The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
The low angle data collected at lower concentration were merged with the highest concentration high angle data to yield the final composite scattering curve.
Merged SAXS scattering curve of the Pro-CPG2-2 pro-enzyme design of CP-N89 circular permutant of carboxypeptidase G2 with the K177A (wild-type residue numbering) mutation in the presence of methotrexate. (Methotrexate is expected to have been converted to its cleaved form prior to data collection.) X-ray wavelength: UNKNOWN. |
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