1GCJ
N-TERMINAL FRAGMENT OF IMPORTIN-BETA
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SPRING-8 BEAMLINE BL45XU |
Synchrotron site | SPring-8 |
Beamline | BL45XU |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-02-25 |
Detector | RIGAKU RAXIS IV++ |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 81.830, 103.780, 126.940 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.180 - 2.600 |
Rwork | 0.215 |
R-free | 0.27000 |
Structure solution method | MAD |
RMSD bond length | 0.006 |
RMSD bond angle | 1.115 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MLPHARE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 57.330 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.072 | 0.293 |
Total number of observations | 271717 * | |
Number of reflections | 33562 | |
<I/σ(I)> | 11.1 | |
Completeness [%] | 99.5 | 99.9 |
Redundancy | 8.1 | 7.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 * | 4 * | drop consists of equal amounts of protein and reservoir solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 40 (mg/ml) | |
2 | 1 | drop | phosphate | 25 (mM) | |
3 | 1 | drop | 2-mercaptoethanol | 5 (mM) | |
4 | 1 | drop | glycerol | 10 (%(v/v)) | |
5 | 1 | reservoir | cacodylic acid | 50 (mM) | |
6 | 1 | reservoir | PEG4000 | 15 (%(w/v)) | |
7 | 1 | reservoir | glycerol | 20 (%) |