2ES3
Crystal Structure of Thrombospondin-1 N-terminal Domain in P1 Form at 1.85A Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2004-04-01 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.07812 |
| Spacegroup name | P 1 |
| Unit cell lengths | 40.024, 41.709, 59.986 |
| Unit cell angles | 73.63, 89.59, 75.73 |
Refinement procedure
| Resolution | 24.430 - 1.850 |
| R-factor | 0.18996 |
| Rwork | 0.187 |
| R-free | 0.24980 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | PDB code: 1Z78 |
| RMSD bond length | 0.018 |
| RMSD bond angle | 1.814 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.950 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Rmerge | 0.051 | 0.240 |
| Number of reflections | 29466 | |
| <I/σ(I)> | 21.08 | 2.91 |
| Completeness [%] | 94.0 | 75.4 |
| Redundancy | 2.4 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 298 | 30% PEG1500 and 0.1M Sodium Acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
