Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL1-5 |
| Synchrotron site | SSRL |
| Beamline | BL1-5 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-06-06 |
| Wavelength(s) | 1.5418 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 68.877, 71.103, 84.302 |
| Unit cell angles | 90.00, 90.14, 90.00 |
Refinement procedure
| Resolution | 29.111 - 1.850 |
| R-factor | 0.1877 |
| Rwork | 0.186 |
| R-free | 0.24430 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2ocj |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.057 |
| 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] | 42.700 | 1.920 |
| High resolution limit [Å] | 1.850 | 1.850 |
| Number of reflections | 68919 | |
| <I/σ(I)> | 8.6 | 2.6 |
| Completeness [%] | 98.9 | 97.9 |
| Redundancy | 3.57 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.6 | 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(200 mM lithium acetate, 20% (w/v) PEG 3350), VAPOR DIFFUSION, SITTING DROP, temperature 277K |
