1UU2
Histidinol-phosphate aminotransferase (HisC) from Thermotoga maritima (apo-form)
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE X13 |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | X13 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2003-08-15 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.646, 98.560, 124.585 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 * - 2.800 |
| R-factor | 0.236 |
| Rwork | 0.236 |
| R-free | 0.28800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h1c |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.414 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.900 |
| High resolution limit [Å] | 2.850 * | 2.800 |
| Rmerge | 0.098 * | 0.441 * |
| Total number of observations | 57136 * | |
| Number of reflections | 15921 | |
| <I/σ(I)> | 9.6 | 1.8 |
| Completeness [%] | 91.7 | 99.3 |
| Redundancy | 2.5 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, sitting drop * | 7.5 * | 20 * | pH 7.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | HEPES | 10 (mM) | pH7.5 |
| 2 | 1 | drop | dithiothreitol | 10 (mM) | |
| 3 | 1 | drop | EDTA | 2 (mM) | |
| 4 | 1 | drop | protein | 35 (mg/ml) | |
| 5 | 1 | reservoir | ethylene glycol | 40 (%(v/v)) | |
| 6 | 1 | reservoir | sodium acetate | 0.1 (M) | pH6.2 |
