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 |