2Q1E
Altered dimer interface decreases stability in an amyloidogenic kappa1 Bence Jones protein.
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-BM |
| Synchrotron site | APS |
| Beamline | 19-BM |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-02-07 |
| Detector | SBC-3 |
| Wavelength(s) | 1.0718 |
| Spacegroup name | P 41 3 2 |
| Unit cell lengths | 176.054, 176.054, 176.054 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 35.210 - 2.550 |
| R-factor | 0.1662 |
| Rwork | 0.165 |
| R-free | 0.20601 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Vk1 O18/O8 germline variable light chain domain monomer |
| RMSD bond length | 0.020 |
| RMSD bond angle | 1.832 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 176.000 | 2.640 |
| High resolution limit [Å] | 2.550 | 2.550 |
| Number of reflections | 29819 | |
| <I/σ(I)> | 82.5 | 9.8 |
| Completeness [%] | 99.3 | 93 |
| Redundancy | 98.7 | 68.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 | 295 | Mother Liquor: 15-30% (w/v) PEG 4K, 0.2 M Li2SO4, 0.1 M TRIS pH 7.9-8.9. Protein: 890 micromolar in 10 mM TRIS, pH 7.4, VAPOR DIFFUSION, HANGING DROP, temperature 295K |
