3UW5
Crystal structure of the BIR domain of MLIAP bound to GDC0152
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-1 |
| Synchrotron site | SSRL |
| Beamline | BL9-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-07-19 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.97946 |
| Spacegroup name | P 41 21 2 |
| Unit cell lengths | 87.396, 87.396, 73.466 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 1.710 |
| R-factor | 0.15656 |
| Rwork | 0.156 |
| R-free | 0.16580 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.138 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.6.0117) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.770 |
| High resolution limit [Å] | 1.710 | 1.710 |
| Number of reflections | 31343 | |
| <I/σ(I)> | 13.9 | 4 |
| Completeness [%] | 99.8 | 100 |
| Redundancy | 7.9 | 8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION | 6 | 292 | Protein at 25 mg/mL in 10 mM MES was mixed with peptide (AVPW)n a 1:2 protein/peptide ratio. The MLIAP peptide complex was mixed with crystallization well solution (100 mM Bis tris(hydroxymethyl)aminomethane (tris), pH 6; 200 mM lithium sulfate; 20 25% (w/v) poly(ethylene glycol) 3350) in a ratio of 1 uL of protein complex to 1 uL of well solution, VAPOR DIFFUSION, temperature 292K |
