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Optics Comparison: Superbends 8.3.1 vs. 12.3.1 in Protein Crystal Macromolecular X-ray Crystallography

Explore the comparison between optics Superbend 8.3.1 and 12.3.1 for protein crystallography, focusing on mirrors, convergence angles, spectral dispersions, and bandpass adjustments. Discover the nuances in resolution and performance factors. This study by MacDowell et al. (2004) provides insights for advanced X-ray crystallography setups.

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Optics Comparison: Superbends 8.3.1 vs. 12.3.1 in Protein Crystal Macromolecular X-ray Crystallography

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  1. Lattice Comparison Test Superbends 8.3.1 and 12.3.1

  2. ALS 8.3.1 optics Superbend Pt & Rh on invar Plane Parabolic M1 mirror Pt & Rh on Si Torroidal M2 mirror 100 μm aperture Scatter guard ADSC Quantum 315r convergence angle slits two flat Si(111) monochromator Protein Crystal MacDowell et. al. (2004) J. Sync. Rad.11 447-455

  3. 11.1 keV, convergence slits “wide” (3 x 0.3 mRad), pixel = 0.83 μm, FWHM from knife edge

  4. 0.014% Si(111) spectral dispersion 1% multilayer Si(111) vs multilayers 4 Å resolution 1.9 Å

  5. Wide-bandpass MX?

  6. 0.0007 % (8 hours) Existing mono Adjustable bandpass Ge(11 1 1) Si(111) 6 mm 3 mm Ge(11 1 1) 16.26° Si(111) d = 0.51 Å 2θ = 147.478° For 12660 eV

  7. 0.014 % (30 min) Existing mono Adjustable bandpass Ge(11 1 1) Si(111) 3 mm Ge(11 1 1) Si(111)

  8. 1 % (~1 second) Existing mono Adjustable bandpass Ge(11 1 1) 3 mm ML Ge(11 1 1) ML

  9. 0.0007 % (8 hours) Existing mono Adjustable bandpass Ge(11 1 1) 6 mm 3 mm ML Ge(11 1 1) 16.26° ML d = 0.51 Å 2θ = 147.478° For 12660 eV

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