3PTF
X-ray structure of the non-covalent complex between UbcH5A and Ubiquitin
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2006-06-01 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 0.97918 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 27.462, 102.903, 159.806 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.700 |
R-factor | 0.21177 |
Rwork | 0.209 |
R-free | 0.27538 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ubq 1x23 |
RMSD bond length | 0.009 |
RMSD bond angle | 1.095 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.800 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 13156 | |
<I/σ(I)> | 17.4 | 3.2 |
Completeness [%] | 97.4 | 98.3 |
Redundancy | 5.3 | 5.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 292 | Crystals of the complex were grown by hanging-drop vapor diffusion at 19 C by combining 1.5 ul of protein solution (20 mM MES pH 6.0, 150 mM NaCl and 0.5 mM TCEP) at 20 mg/ml with 1.5 ul of reservoir solution (0.1 M Tris pH 8.5 and 24% PEG 10,000), VAPOR DIFFUSION, HANGING DROP, temperature 292K |