1I7K
CRYSTAL STRUCTURE OF HUMAN MITOTIC-SPECIFIC UBIQUITIN-CONJUGATING ENZYME, UBCH10
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU RU200 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 2000-06-29 |
Detector | RIGAKU RAXIS IV |
Wavelength(s) | 1.5418 |
Spacegroup name | P 1 |
Unit cell lengths | 40.965, 48.371, 51.763 |
Unit cell angles | 62.66, 75.26, 81.99 |
Refinement procedure
Resolution | 50.000 - 1.950 |
Rwork | 0.176 |
R-free | 0.22600 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2e2c |
RMSD bond length | 0.012 |
RMSD bond angle | 1.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.010 |
High resolution limit [Å] | 1.940 | 1.940 |
Rmerge | 0.061 | 0.319 |
Number of reflections | 24518 | 2218 * |
<I/σ(I)> | 25.6 | 4.167 |
Completeness [%] | 97.7 | 88.8 |
Redundancy | 2.9 | 2.532 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7 | 20 * | drop consists of equal amounts of protein and precipitant solutions * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 10 (mg/ml) | |
2 | 1 | reservoir | PEG1500 | 30 (%) |