1M21
Crystal structure analysis of the peptide amidase PAM in complex with the competitive inhibitor chymostatin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-07-12 |
Detector | MARRESEARCH |
Wavelength(s) | 0.934 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 74.598, 62.559, 102.382 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 100.000 * - 1.800 |
R-factor | 0.203 |
Rwork | 0.203 |
R-free | 0.21600 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1m22 |
RMSD bond length | 0.007 * |
RMSD bond angle | 1.389 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 60.290 | 1.910 |
High resolution limit [Å] | 1.780 * | 1.800 |
Rmerge | 0.099 | 0.273 |
Number of reflections | 89189 * | |
<I/σ(I)> | 6.1 | 3 |
Completeness [%] | 98.1 * | 79.9 |
Redundancy | 3.7 | 2.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 289 | Neumann, S., (2002) Acta Crystallogr., Sect.D, 58, 333. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 13 (%) | |
2 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |
3 | 1 | reservoir | glycerine | 20 (%) | |
4 | 1 | reservoir | sodium azide | 0.02 (%) | |
5 | 1 | drop | protein | 24 (mg/ml) |