3NRX
Insights into anti-parallel microtubule crosslinking by PRC1, a conserved non-motor microtubule binding protein
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 24-ID-E |
Synchrotron site | APS |
Beamline | 24-ID-E |
Temperature [K] | 173 |
Detector technology | CCD |
Collection date | 2009-04-21 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 32 |
Unit cell lengths | 49.078, 49.078, 94.784 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 25.000 - 1.750 |
R-factor | 0.202 |
Rwork | 0.198 |
R-free | 0.26900 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3nry |
RMSD bond length | 0.008 |
RMSD bond angle | 1.030 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.810 |
High resolution limit [Å] | 1.750 | 1.750 |
Rmerge | 0.053 | 0.361 |
Number of reflections | 24182 | |
<I/σ(I)> | 31.4 | 2.62 |
Completeness [%] | 94.0 | 94.8 |
Redundancy | 4.3 | 4.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 9.5 | 277 | 1:1 v/v of protein ( 50 mg/ml in 80 mM PIPES, pH6.8, 1 mM MgCl2, 1 mM EDTA and 150 mM KCl) and reservoir buffer (100 mM CHES, pH 9.5, 30% PEG3000), VAPOR DIFFUSION, HANGING DROP, temperature 277K |