5M2M
Complex between human TNF alpha and Llama VHH3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-10-18 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.931 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 145.380, 83.844, 150.063 |
| Unit cell angles | 90.00, 128.77, 90.00 |
Refinement procedure
| Resolution | 29.590 - 2.300 |
| R-factor | 0.2128 |
| Rwork | 0.211 |
| R-free | 0.24750 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5m2i |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.110 |
| Data reduction software | XDS |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | BUSTER (2.10.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.420 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.090 | 0.320 |
| Number of reflections | 62613 | |
| <I/σ(I)> | 11.2 | 4.1 |
| Completeness [%] | 99.9 | 99.9 |
| Redundancy | 4.1 | 4 |
| CC(1/2) | 0.960 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | mixing 100 to 300 nL of protein (9 mg per ml in HEPES 10 mM pH 7.0) with 100 nL of precipitant solution containing: 9% PEG3350, 8% PEG-MME550, 130 mM NaSO4, 70 mM BTP, 30 mM Mes, and 3 mM ZnSO4, 8.5 |
