1QQ5
STRUCTURE OF L-2-HALOACID DEHALOGENASE FROM XANTHOBACTER AUTOTROPHICUS
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-3 |
| Synchrotron site | ESRF |
| Beamline | ID14-3 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1998-04 |
| Detector | MARRESEARCH |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 57.050, 83.928, 91.227 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 20.000 - 1.520 |
| R-factor | 0.198 * |
| Rwork | 0.204 |
| R-free | 0.23200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1aq6 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 21.400 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | CNS (0.5) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.550 |
| High resolution limit [Å] | 1.520 | 1.520 |
| Rmerge | 0.064 | 0.351 |
| Total number of observations | 306585 * | |
| Number of reflections | 63057 | |
| <I/σ(I)> | 24.7 | |
| Completeness [%] | 92.7 | 81.4 |
| Redundancy | 4.9 | 2.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7 | used to seeding, Ridder, I.S., (1995) Protein Sci., 4, 2619. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 2.5 (mg/ml) | |
| 2 | 1 | drop | PEG8000 | 15 (%) | |
| 3 | 1 | drop | sodium formate | 200 (mM) | |
| 4 | 1 | drop | Bis-Tris | 100 (mM) | |
| 5 | 1 | reservoir | PEG8000 | 20 (%) | |
| 6 | 1 | reservoir | sodium formate | 200 (mM) | |
| 7 | 1 | reservoir | bis-Tris | 100 (mM) |
