1QMN
Alpha1-antichymotrypsin serpin in the delta conformation (partial loop insertion)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SRS BEAMLINE PX7.2 |
| Synchrotron site | SRS |
| Beamline | PX7.2 |
| Temperature [K] | 293 |
| Detector technology | IMAGE PLATE |
| Collection date | 1999-02-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 41.723, 122.094, 41.724 |
| Unit cell angles | 90.00, 101.03, 90.00 |
Refinement procedure
| Resolution | 40.950 - 2.270 |
| R-factor | 0.197 |
| Rwork | 0.197 |
| R-free | 0.24300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1as4 |
| RMSD bond length | 0.036 |
| RMSD bond angle | 23.500 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 41.000 | 2.390 |
| High resolution limit [Å] | 2.300 | 2.270 |
| Rmerge | 0.101 | 0.343 |
| Total number of observations | 18805 * | |
| Number of reflections | 11373 | |
| <I/σ(I)> | 4.4 | 2.4 |
| Completeness [%] | 62.1 | 17.2 |
| Redundancy | 1.7 | 1.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.4 * | 18 * | 1 MICROLITER OF 10MG/ML PROTEIN IN 50MM TRIS, 50MM KCL, PH 7.4 WAS MIXED WITH 2 MICROLITER OF PRECIPITANT AND EQUILIBRATED AS A HANGING DROP OVER 1ML OF PRECIPITANT (20% [W/V] PEG 4000, 0.2M AMMONIUM SULPHATE, 0.1M NAOAC, PH 4.5), AT 18 DEGREES C |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | Tris | 50 (mM) | |
| 3 | 1 | drop | 50 (mM) | ||
| 4 | 1 | reservoir | PEG4000 | 20 (%(w/v)) | |
| 5 | 1 | reservoir | ammonium sulfate | 0.2 (M) | |
| 6 | 1 | reservoir | 0.1 (M) |
