1VDE
PI-SCEI, A HOMING ENDONUCLEASE WITH PROTEIN SPLICING ACTIVITY
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X4A |
Synchrotron site | NSLS |
Beamline | X4A |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1996-09 |
Wavelength(s) | 0.9656, 0.9794 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 59.750, 102.400, 87.100 |
Unit cell angles | 90.00, 94.10, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.400 |
R-factor | 0.192 |
Rwork | 0.192 |
R-free | 0.23800 |
Structure solution method | MAD |
RMSD bond length | 0.140 |
RMSD bond angle | 24.900 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MADSYS |
Refinement software | X-PLOR (3.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 10.000 * | 2.500 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.060 * | |
Number of reflections | 77252 | |
<I/σ(I)> | 19.9 | 11.5 |
Completeness [%] | 96.7 | 97.3 |
Redundancy | 3 | 3.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | 4% PEG 6K, 10MM BME, 3MM CDCL2, 1MM MGCL2, 100MM TRIS, PH=8.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | PEG6000 | 4 (%) | |
10 | 1 | drop | 0.5 (mM) | ||
11 | 1 | drop | Tris | 60 (mM) | |
2 | 1 | reservoir | beta-mercaptoethanol | 10 (mM) | |
3 | 1 | reservoir | 3 (mM) | ||
4 | 1 | reservoir | 1 (mM) | ||
5 | 1 | reservoir | Tris | 100 (mM) | |
6 | 1 | drop | protein | 4 (mg/ml) | |
7 | 1 | drop | PEG6000 | 2 (%) | |
8 | 1 | drop | beta-mercaptoethanol | 7.5 (mM) | |
9 | 1 | drop | 1.5 (mM) |