1GL0
structure of the complex between bovine alpha-chymotrypsin and PMP-D2v, an inhibitor from the insect Locusta migratoria
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | LURE BEAMLINE DW32 |
| Synchrotron site | LURE |
| Beamline | DW32 |
| Temperature [K] | 300 |
| Collection date | 1997-11-15 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 85.853, 85.853, 187.983 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 14.980 - 3.000 |
| R-factor | 0.164 * |
| Rwork | 0.174 |
| R-free | 0.19300 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1cho |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.320 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | X-PLOR |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 15.000 | 3.100 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.151 | 0.423 |
| Number of reflections | 8699 | |
| Completeness [%] | 99.8 | 99.9 |
| Redundancy | 7.3 | 7.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 5 | 20 * | 0.1 M NA ACETATE PH 5.0, 29% PEG 400, 0.1 M CDCL2 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | sodium acetate | 100 (mM) | |
| 2 | 1 | reservoir | PEG400 | 29 (%) | |
| 3 | 1 | reservoir | 100 (mM) | pH5.0 | |
| 4 | 1 | drop | protein | 10 (mg/ml) |
