3UII
crystal structure of human Survivin in complex with H3(1-10) peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-E |
| Synchrotron site | APS |
| Beamline | 24-ID-E |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2011-02-11 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 0.9792 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 115.250, 71.256, 81.636 |
| Unit cell angles | 90.00, 128.46, 90.00 |
Refinement procedure
| Resolution | 29.272 - 2.600 |
| R-factor | 0.2247 |
| Rwork | 0.222 |
| R-free | 0.27340 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1f3h |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.430 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | PHENIX |
| Refinement software | PHENIX ((phenix.refine: 1.6.4_486)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.690 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.086 | 0.529 |
| Number of reflections | 16412 | |
| <I/σ(I)> | 10.1 | 2 |
| Completeness [%] | 98.9 | 96.4 |
| Redundancy | 4 | 3.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 293 | 0.1 M ammonium citrate tribasic, pH 7.0, 12% PEG 3350, VAPOR DIFFUSION, HANGING DROP, temperature 293K |
