2PF5
Crystal Structure of the Human TSG-6 Link Module
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-2 |
| Synchrotron site | ESRF |
| Beamline | ID14-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-08-27 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.933 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 134.816, 75.870, 90.674 |
| Unit cell angles | 90.00, 103.42, 90.00 |
Refinement procedure
| Resolution | 88.040 - 1.900 |
| R-factor | 0.19596 |
| Rwork | 0.194 |
| R-free | 0.22588 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1UUH - crystal structure of CD44 |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.660 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | DM |
| Refinement software | REFMAC (5.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 88.040 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.071 | 0.410 |
| Number of reflections | 69439 | |
| <I/σ(I)> | 6.35 | 1.51 |
| Completeness [%] | 99.1 | 98.62 |
| Redundancy | 4.08 | 3.98 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | A 2.5 ul drop formed from equal amounts of protein solution (7 mg/ml solution in approximately 25mM TrisHCl and 75mM NaCl) and well solution was equilibrated against 1 ml well solution (2 M Ammonium Sulphate, 2 % v/v PEG 400 and 0.1M Sodium Hepes (pH 7.5)), VAPOR DIFFUSION, SITTING DROP, temperature 293K |
