7LBP
Crystal structure of human Survivin bound to histone H3T3phK4ac 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 | 113.117, 70.988, 83.322 |
| Unit cell angles | 90.00, 130.04, 90.00 |
Refinement procedure
| Resolution | 35.490 - 2.600 |
| R-factor | 0.2139 |
| Rwork | 0.212 |
| R-free | 0.24720 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3uec |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.377 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| 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 | 2.640 |
| High resolution limit [Å] | 2.600 | 7.050 | 2.600 |
| Rmerge | 0.053 | 0.040 | 0.427 |
| Rmeas | 0.062 | 0.047 | 0.521 |
| Rpim | 0.032 | 0.025 | 0.296 |
| Total number of observations | 58042 | ||
| Number of reflections | 15604 | 797 | 753 |
| <I/σ(I)> | 12 | ||
| Completeness [%] | 99.7 | 97.1 | 99.1 |
| Redundancy | 3.7 | 3.6 | 3 |
| CC(1/2) | 0.991 | 0.879 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 289 | 1 uL of protein at 10mg/mL was mixed with 1 uL of buffer composed of 0.16 M potassium/sodium tartrate, 12% PEG 3350 |
