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) |