1TW6
Structure of an ML-IAP/XIAP chimera bound to a 9mer peptide derived from Smac
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | CHESS BEAMLINE A1 |
| Synchrotron site | CHESS |
| Beamline | A1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-09-09 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 87.856, 87.856, 74.634 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.750 - 1.713 |
| R-factor | 0.15595 |
| Rwork | 0.155 |
| R-free | 0.17088 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1OXN (without peptide) |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.127 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.770 |
| High resolution limit [Å] | 1.710 | 1.710 |
| Rmerge | 0.115 | 0.664 |
| Number of reflections | 31742 | |
| <I/σ(I)> | 21.4 | 2.1 |
| Completeness [%] | 98.5 | 88.2 |
| Redundancy | 12 | 7.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 298 | lithium sulfate, Bis-tris, PEG 3350, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
