2X89
Structure of the Beta2_microglobulin involved in amyloidogenesis
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID29 |
| Synchrotron site | ESRF |
| Beamline | ID29 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Detector | ADSC CCD |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 77.490, 100.864, 83.743 |
| Unit cell angles | 90.00, 106.43, 90.00 |
Refinement procedure
| Resolution | 19.850 - 2.160 |
| R-factor | 0.23962 |
| Rwork | 0.238 |
| R-free | 0.26691 |
| Structure solution method | SAD |
| Starting model (for MR) | 1bmg |
| RMSD bond length | 0.028 |
| RMSD bond angle | 2.439 |
| Data reduction software | HKL |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.240 |
| High resolution limit [Å] | 2.160 | 2.160 |
| Rmerge | 0.070 | 0.320 |
| Number of reflections | 66127 | |
| <I/σ(I)> | 14.6 | 3.1 |
| Completeness [%] | 99.3 | 99 |
| Redundancy | 3.7 | 3.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 6%PEG4000, 0.2M AMMONIUM SULPHATE, 0.1M NA-ACETEATE PH4.6 |
