Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | AUSTRALIAN SYNCHROTRON BEAMLINE MX2 |
Synchrotron site | Australian Synchrotron |
Beamline | MX2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-10-18 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | H 3 2 |
Unit cell lengths | 128.365, 128.365, 228.412 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 42.290 - 2.600 |
R-factor | 0.1786 |
Rwork | 0.177 |
R-free | 0.21572 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ZGR |
RMSD bond length | 0.007 |
RMSD bond angle | 1.189 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 42.200 | 2.740 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.140 | 0.780 |
Number of reflections | 22546 | |
<I/σ(I)> | 12.8 | 3.3 |
Completeness [%] | 99.9 | 99.9 |
Redundancy | 11.1 | 11.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7.4 | THE PROTEIN WAS DIALYSED AGAINST HEPES BUFFER WITH MELAMINE AND THE FINAL CONCENTRATION OF PROTEIN WAS 2 MG/ML. THIS COMPLEX WAS SET UP IN A 3:2 RATIO WITH 147 MM NACL, 32% V/V PEG 400 AND 100 MM HEPES PH 7.4. |