1IU9
Crystal structure of the C-terminal domain of aspartate racemase from Pyrococcus horikoshii OT3
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 90 |
| Detector technology | CCD |
| Collection date | 2001-02-28 |
| Detector | MARRESEARCH |
| Wavelength(s) | 1.000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 36.829, 45.328, 57.366 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 100.000 * - 2.040 |
| R-factor | 0.225 |
| Rwork | 0.225 |
| R-free | 0.27100 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | C-terminal domain in the intact structure of aspartate racemase from Pyrococcus horikoshii OT3 |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.070 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | AMoRE |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 100.000 * | 2.150 |
| High resolution limit [Å] | 2.040 | 2.040 |
| Rmerge | 0.108 | 0.252 |
| Total number of observations | 57302 * | |
| Number of reflections | 6508 * | |
| <I/σ(I)> | 5.2 | 3 |
| Completeness [%] | 99.3 | 96.3 |
| Redundancy | 5.4 | 5.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 * | 20 * | 16% Peg8000, 0.10M MES, 0.2M Calcium acetate, pH 6.5, VAPOR DIFFUSION, SITTING DROP, temperature 293.2K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 30 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 50 (mM) | pH8.0 |
| 3 | 1 | drop | mercaptoethanol | 2 (mM) | |
| 4 | 1 | reservoir | PEG8000 | 16 (%) | |
| 5 | 1 | reservoir | MES | 0.10 (M) | pH6.5 |
| 6 | 1 | reservoir | calcium acetate | 0.20 (M) |
