2C7N
Human Rabex-5 residues 1-74 in complex with Ubiquitin
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM14 |
Synchrotron site | ESRF |
Beamline | BM14 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-09-16 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 44.300, 68.900, 98.500 |
Unit cell angles | 108.20, 102.70, 90.40 |
Refinement procedure
Resolution | 20.000 - 2.100 |
R-factor | 0.198 |
Rwork | 0.195 |
R-free | 0.23800 |
Structure solution method | MAD |
RMSD bond length | 0.020 * |
RMSD bond angle | 1.800 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | HKL2MAP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.200 |
High resolution limit [Å] | 2.100 | 2.100 |
Rmerge | 0.033 * | 0.169 * |
Number of reflections | 57954 | |
<I/σ(I)> | 12.7 | 3.5 |
Completeness [%] | 92.3 | 66.4 |
Redundancy | 2.7 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 20 * | SITTING DROP 300NL PLUS 300NL 0.2M AMMONIUM ACETATE 0.1M NACITRATE PH 6.5 25% PEG400 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | reservoir | ammonium acetate | 0.2 (M) | |
3 | 1 | reservoir | sodium citrate | 0.1 (M) | |
4 | 1 | reservoir | PEG4000 | 25 (%) |