2ERF
Crystal Structure of the Thrombospondin-1 N-terminal Domain at 1.45A 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 | 2005-07-07 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 1.00931 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 43.310, 40.489, 60.086 |
| Unit cell angles | 90.00, 106.99, 90.00 |
Refinement procedure
| Resolution | 22.860 - 1.450 |
| R-factor | 0.18559 |
| Rwork | 0.183 |
| R-free | 0.21672 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1z78 |
| RMSD bond length | 0.011 |
| RMSD bond angle | 1.467 |
| 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 | 1.500 |
| High resolution limit [Å] | 1.450 | 1.450 |
| Rmerge | 0.068 | 0.376 |
| Number of reflections | 34155 | |
| <I/σ(I)> | 39.7 | 2.5 |
| Completeness [%] | 95.8 | 68.7 |
| Redundancy | 3.8 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 4.6 | 300 | 30% PEG1500 and 0.1M Sodium Acetate, pH 4.6, VAPOR DIFFUSION, HANGING DROP, temperature 300K |
