1R1L
Structure of dimeric antithrombin complexed with a P14-P9 reactive loop peptide and an exogenous tripeptide (formyl-norleucine-LF)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX14.2 |
| Synchrotron site | SRS |
| Beamline | PX14.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2002-12-04 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.171, 100.421, 87.198 |
| Unit cell angles | 90.00, 104.29, 90.00 |
Refinement procedure
| Resolution | 24.990 - 2.700 |
| Rwork | 0.204 |
| R-free | 0.24900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1lk6 |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.300 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((TRUNCATE)) |
| Phasing software | CNS |
| Refinement software | CNS |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 25.080 | 2.870 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.163 | 0.053 |
| Number of reflections | 31707 | |
| <I/σ(I)> | 4.6 | 1.6 |
| Completeness [%] | 99.6 | 99.5 |
| Redundancy | 3.1 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.8 | 298 | PEG 4000, sodium cacodylate, ammonium fluoride, glycerol, pH 6.8, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
