Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 4.2.2 |
| Synchrotron site | ALS |
| Beamline | 4.2.2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-06-22 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 69.164, 69.213, 83.851 |
| Unit cell angles | 90.00, 90.11, 90.00 |
Refinement procedure
| Resolution | 53.378 - 2.500 |
| R-factor | 0.1813 |
| Rwork | 0.176 |
| R-free | 0.24660 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ocj |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.157 |
| Data reduction software | d*TREK |
| Data scaling software | d*TREK |
| Phasing software | CNS |
| Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 53.378 | 2.590 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Number of reflections | 27431 | |
| <I/σ(I)> | 7.9 | 3.5 |
| Completeness [%] | 99.2 | 96.7 |
| Redundancy | 3.58 | 3.38 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | 2 microliter protein solution (around 5.0-7.0 mg/ml protein in 20 mM Tris pH 7.6, 150 mM NaCl, 10 mM DTT) were mixed with 2 microliter reservoir buffer(100 mM HEPES, 30 % (w/v) polyethylene glycol (PEG) 6000, pH 7.0), VAPOR DIFFUSION, HANGING DROP, temperature 277K |
