3RIP
Crystal Structure of human gamma-tubulin complex protein 4 (GCP4)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SOLEIL BEAMLINE PROXIMA 1 |
Synchrotron site | SOLEIL |
Beamline | PROXIMA 1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-02-11 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.033 |
Spacegroup name | P 63 2 2 |
Unit cell lengths | 214.950, 214.950, 128.660 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
R-factor | 0.22837 |
Rwork | 0.227 |
R-free | 0.25992 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | THE STARTING MODEL WAS SOLVED AND PARTIALLY REFINED FROM SAD DATA COLLECTED USING THE SELENEMETHIONINE PROTEIN |
RMSD bond length | 0.025 |
RMSD bond angle | 2.105 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0072) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 2.400 |
High resolution limit [Å] | 2.300 | 2.300 |
Number of reflections | 73248 | |
<I/σ(I)> | 2.45 | |
Completeness [%] | 99.4 | 99.9 |
Redundancy | 5.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 285 | 8-10% MPD (2-methyl-2,4-pentanediol), 0-20% glycerol (w/v), 300-400 mM Tris-Hcl, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 285K |