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 | 129.230, 129.230, 233.791 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 43.180 - 3.100 |
R-factor | 0.16604 |
Rwork | 0.164 |
R-free | 0.20891 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3ZGR |
RMSD bond length | 0.007 |
RMSD bond angle | 1.144 |
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] | 43.100 | 3.260 |
High resolution limit [Å] | 3.090 | 3.090 |
Rmerge | 0.140 | 0.620 |
Number of reflections | 13929 | |
<I/σ(I)> | 12.9 | 3.6 |
Completeness [%] | 99.5 | 96.5 |
Redundancy | 9.7 | 9.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | THE PROTEIN WAS DIALYSED AGAINST HEPES BUFFER WITH BARBITURIC ACID, THE FINAL CONCENTRATION OF PROTEIN WAS 2 MG/ML AND THIS WAS SET UP IN A 1:1 RATIO AGAINST 180 MM NACL, 31% V/V PEG 400 AND 100 MM HEPES PH 7.0. |