5M2J
Complex between human TNF alpha and Llama VHH2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-10-18 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.931 |
| Spacegroup name | P 63 |
| Unit cell lengths | 87.310, 87.310, 62.730 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 48.280 - 1.900 |
| R-factor | 0.1602 |
| Rwork | 0.158 |
| R-free | 0.19620 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 5m2i |
| RMSD bond length | 0.010 |
| 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] | 48.300 | 1.950 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.035 | 0.100 |
| Number of reflections | 21089 | |
| <I/σ(I)> | 23.5 | 11 |
| Completeness [%] | 97.9 | 94.6 |
| Redundancy | 2.9 | 2.7 |
| CC(1/2) | 0.999 | 0.980 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 293 | 100 to 300 nL of protein at 11 mg per ml in HEPES 10 mM pH 7.0 with 100 nL of precipitant solution containing 12% 130 mM NaCl and 366 mM CaCl2 and 70 mM CAPS pH 9.0 and 30 mM MES pH 8.0 |
