5W89
Crystal structure of human Mcl-1 in complex with modified Bim BH3 peptide SAH-MS1-18
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 | PIXEL |
Collection date | 2017-04-14 |
Detector | DECTRIS EIGER X 16M |
Wavelength(s) | 0.97918 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 43.390, 43.390, 163.430 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 19.405 - 1.420 |
R-factor | 0.1442 |
Rwork | 0.142 |
R-free | 0.18550 |
RMSD bond length | 0.008 |
RMSD bond angle | 0.865 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.11.1_2575) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 19.405 | 19.405 | 1.460 |
High resolution limit [Å] | 1.420 | 6.350 | 1.420 |
Rmerge | 0.083 | 0.053 | 1.326 |
Rmeas | 0.085 | 0.055 | 1.367 |
Total number of observations | 525289 | ||
Number of reflections | 30358 | 385 | 2216 |
<I/σ(I)> | 15.97 | 38.83 | 1.85 |
Completeness [%] | 99.1 | 89.7 | 100 |
Redundancy | 17.304 | 15.574 | 17.233 |
CC(1/2) | 0.999 | 0.999 | 0.728 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 9 | 300 | Reservior: 25% PEG 3350, 50mM Tris pH 9.0, 0.2 M Ammonium acetate; Protein: 408 uM in 20 mM TRis , 10 mM TCEP, 5mM Zn2SO4 |