5IA7
Crystal structure of Ubiquitin fold modifier 1 (Ufm1)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID30B |
Synchrotron site | ESRF |
Beamline | ID30B |
Detector technology | PIXEL |
Detector | DECTRIS PILATUS 6M-F |
Wavelength(s) | 1.00800 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.282, 56.730, 64.450 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.580 - 2.000 |
R-factor | 0.19968 |
Rwork | 0.198 |
R-free | 0.22961 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5iaa |
RMSD bond length | 0.016 |
RMSD bond angle | 1.749 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 64.450 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.142 | |
Number of reflections | 11636 | |
<I/σ(I)> | 7.1 | |
Completeness [%] | 99.3 | |
Redundancy | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 293.15 | 0.2M Ammonium acetate, 0.1M Sodium citrate tribasic dihydrate and 30% PEG 4000 |