4GSW
Crystal structure of ubiquitin from Entamoeba histolytica to 2.15 Angstrom
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2012-04-08 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 38.631, 49.865, 76.824 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 34.513 - 2.150 |
R-factor | 0.1994 |
Rwork | 0.193 |
R-free | 0.25610 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ubq |
RMSD bond length | 0.014 |
RMSD bond angle | 1.493 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX (AutoMR) |
Refinement software | PHENIX ((phenix.refine: 1.8_1069)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.170 |
High resolution limit [Å] | 2.150 | 2.150 |
Rmerge | 0.085 | 0.279 |
Number of reflections | 8430 | |
<I/σ(I)> | 13.6 | 3.1 |
Completeness [%] | 98.1 | 96.8 |
Redundancy | 3.5 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 291 | EhUbiquitin at 13 mg/mL in S200 buffer was mixed 1:1 with and equilibrated against crystallization solution containing 22% (w/v) PEG 3350, 200 mM LiSO4, and 100 mM Bis-Tris, pH 5.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K |