3V31
Crystal Structure of the Peptide Bound Complex of the Ankyrin Repeat Domains of Human ANKRA2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-04-14 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97931 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 29.663, 52.822, 51.556 |
| Unit cell angles | 90.00, 98.01, 90.00 |
Refinement procedure
| Resolution | 26.410 - 1.570 |
| R-factor | 0.1759 |
| Rwork | 0.174 |
| R-free | 0.20450 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3so8 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.223 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (refmac_5.5.0109) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 1.630 |
| High resolution limit [Å] | 1.570 | 3.380 | 1.570 |
| Rmerge | 0.041 | 0.027 | 0.214 |
| Number of reflections | 22107 | ||
| <I/σ(I)> | 16.8 | ||
| Completeness [%] | 99.8 | 99 | 99 |
| Redundancy | 4.4 | 4.3 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 291 | 0.1M Bis-Tris, pH 6.5, 0.2M NaCl, 25% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 291K |
