2XPH
Crystal structure of human SENP1 with the bound cobalt
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-02-13 |
Detector | ADSC CCD |
Spacegroup name | P 31 2 1 |
Unit cell lengths | 71.172, 71.172, 199.988 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 66.660 - 2.400 |
R-factor | 0.23137 |
Rwork | 0.227 |
R-free | 0.31339 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2iyc |
RMSD bond length | 0.016 |
RMSD bond angle | 1.639 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 45.000 | 2.530 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.090 | 0.430 |
Number of reflections | 23808 | |
<I/σ(I)> | 8.5 | 2.5 |
Completeness [%] | 99.8 | 100 |
Redundancy | 5.1 | 5.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | CRYSTALS FORMED FROM 1 TO 1 OF RESERVOIR SOLUTION (1.8 M AMMONIUM SULFATE, 50 MM COCL2 AND 100 MM MES PH 6.5) AND PROTEIN SOLUTION (20 MG/ML IN 20 MM TRIS/HCL (PH 8.0), AND 50 MM NACL). |