1AUW
H91N DELTA 2 CRYSTALLIN FROM DUCK
Experimental procedure
Source type | SYNCHROTRON |
Source details | CHESS BEAMLINE F1 |
Synchrotron site | CHESS |
Beamline | F1 |
Temperature [K] | 80 |
Detector technology | IMAGE PLATE |
Collection date | 1995-01 |
Detector | FUJI |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 94.100, 100.200, 109.100 |
Unit cell angles | 90.00, 102.10, 90.00 |
Refinement procedure
Resolution | 8.000 - 2.500 |
R-factor | 0.161 |
Rwork | 0.161 |
R-free | 0.23500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | TURKEY DELTA 1 CRYSTALLINE |
RMSD bond length | 0.006 |
RMSD bond angle | 19.920 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | X-PLOR (3.8) |
Refinement software | X-PLOR (3.8) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 2.600 |
High resolution limit [Å] | 2.500 | 2.500 |
Rmerge | 0.103 * | 0.330 * |
Total number of observations | 239855 * | |
Number of reflections | 65641 | |
Completeness [%] | 95.0 | 92.6 |
Redundancy | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 | PROTEIN WAS CRYSTALLIZED FROM 18-20% PEG MME 2K, 300 MM MGCL2,100 MM TRIS-HCL PH 8.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 7-8 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 50 (mM) | |
3 | 1 | drop | PEG MME2000 | 9-10 (%(w/v)) | |
4 | 1 | drop | 150 (mM) | ||
5 | 1 | drop | Tris-HCl | 50 (mM) | |
6 | 1 | reservoir | PEG MME2000 | 18-20 (%(w/v)) | |
7 | 1 | reservoir | 300 (mM) | ||
8 | 1 | reservoir | Tris-HCl | 100 (mM) |