1ILW
Crystal Structure of Pyrazinamidase/Nicotinamidase of Pyrococcus horikoshii
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2000-03-01 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.08 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 32.977, 43.418, 55.781 |
| Unit cell angles | 90.00, 101.22, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.050 |
| R-factor | 0.181 * |
| Rwork | 0.181 |
| R-free | 0.25700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | a structure of the same protein obtained on MAD data |
| RMSD bond length | 0.007 * |
| RMSD bond angle | 1.600 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SOLVE |
| Refinement software | SHELXL-97 |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.110 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.027 * | 0.093 * |
| Number of reflections | 9862 | |
| <I/σ(I)> | 42.5 | 17.4 |
| Completeness [%] | 99.2 | 88 |
| Redundancy | 4.246 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 * | 298 | 22.5% PEG3350, 250 mM ammonium acetate, 100 mM sodium acetate, pH 4.6. Seeding., VAPOR DIFFUSION, HANGING DROP, temperature 298K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 20 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 20 (mM) | pH7.5 |
| 3 | 1 | drop | EDTA | 1 (mM) | |
| 4 | 1 | reservoir | sodium acetate | 100 (mM) | pH4.6 |
| 5 | 1 | reservoir | ammonium sulfate | 250 (mM) | |
| 6 | 1 | reservoir | PEG3350 | 22.5 (%) |
