5U52
2 helix minimized version of the B-domain from Protein A (Z34C0 bound to IgG1 Fc (monoclinic form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE A1 |
| Synchrotron site | CHESS |
| Beamline | A1 |
| Temperature [K] | 170 |
| Detector technology | CCD |
| Collection date | 1996-10-24 |
| Detector | PRINCETON 2K |
| Wavelength(s) | 0.95 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 58.392, 76.390, 66.202 |
| Unit cell angles | 90.00, 112.99, 90.00 |
Refinement procedure
| Resolution | 19.358 - 1.942 |
| R-factor | 0.1919 |
| Rwork | 0.190 |
| R-free | 0.22750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1fc1 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.064 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK (1.5.10) |
| Refinement software | PHENIX (1.9_1692) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.020 |
| High resolution limit [Å] | 1.942 | 1.942 |
| Rmerge | 0.224 | |
| Number of reflections | 65918 | |
| <I/σ(I)> | 15 | 4.3 |
| Completeness [%] | 94.8 | 94.1 |
| Redundancy | 1.8 | 1.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 293 | 20% PEG monomethyl ether 550, 0.1M bis-tris propane pH 6.5, 0.1M NaCl, 5mg/mL protein concentration. |
