1LK6
Structure of dimeric antithrombin complexed with a P14-P9 reactive loop peptide and an exogenous tripeptide
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 | 2002-01-30 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.978 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.811, 99.908, 87.292 |
| Unit cell angles | 90.00, 104.44, 90.00 |
Refinement procedure
| Resolution | 34.000 * - 2.800 |
| Rwork | 0.202 |
| R-free | 0.26600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Dimeric antithrombin complexed with a P14-P8 reactive loop peptide and an exogenous tetrapeptide (1jvq). Both peptides omitted in starting model |
| 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] | 37.580 | 2.950 |
| High resolution limit [Å] | 2.800 | 2.800 |
| Rmerge | 0.104 | 0.551 |
| Total number of observations | 91051 * | |
| Number of reflections | 27376 | |
| <I/σ(I)> | 7.5 | 1.7 |
| Completeness [%] | 96.7 | 81.5 |
| Redundancy | 3.3 | 2.5 |
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 at 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 14 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 10-20 (%) | |
| 3 | 1 | reservoir | sodium cacodylate | 50 (mM) | pH6.8 |
| 4 | 1 | reservoir | 0.2 (M) | ||
| 5 | 1 | reservoir | glycerol | 12 (%) | or without |
