2I3H
Structure of an ML-IAP/XIAP chimera bound to a 4-mer peptide (AVPW)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-08-15 |
Detector | SBC |
Wavelength(s) | 1.0332 |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 87.541, 87.541, 73.876 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.620 |
R-factor | 0.16185 |
Rwork | 0.161 |
R-free | 0.17965 |
Structure solution method | FOURIER SYNTHESIS |
Starting model (for MR) | 1.3 A structure of the ML-IAP/XIAP protein bound to a different peptidomimetic with the ligand and surrounding waters removed |
RMSD bond length | 0.009 |
RMSD bond angle | 1.132 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.680 |
High resolution limit [Å] | 1.620 | 1.620 |
Rmerge | 0.068 | 0.406 |
Number of reflections | 32349 | |
<I/σ(I)> | 20.9 | 1.7 |
Completeness [%] | 87.2 | 38.5 |
Redundancy | 5.9 | 0.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | Lithium sulfate, PEG 3350, Bis-tris, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |