7LBO
Crystal structure of human Survivin bound to histone H3 T3phK4me1 peptide
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-06-20 |
| Detector | RAYONIX MX-300 |
| Wavelength(s) | 0.97856 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 114.182, 71.441, 82.786 |
| Unit cell angles | 90.00, 129.11, 90.00 |
Refinement procedure
| Resolution | 34.340 - 2.500 |
| R-factor | 0.2097 |
| Rwork | 0.207 |
| R-free | 0.26060 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3uec |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.457 |
| Data reduction software | HKL-3000 |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 50.000 | 50.000 | 2.540 |
| High resolution limit [Å] | 2.500 | 6.780 | 2.500 |
| Rmerge | 0.043 | 0.028 | 0.329 |
| Rmeas | 0.051 | 0.033 | 0.382 |
| Rpim | 0.026 | 0.017 | 0.193 |
| Total number of observations | 67635 | ||
| Number of reflections | 17812 | 879 | 897 |
| <I/σ(I)> | 14.8 | ||
| Completeness [%] | 99.5 | 94.3 | 100 |
| Redundancy | 3.8 | 3.5 | 3.8 |
| CC(1/2) | 0.998 | 0.954 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 1 uL of protein at 10 mg/mL was mixed with 1 uL of buffer composed of 0.16 M potassium/sodium tartrate, 12% PEG 3350 |
