1REG
CRYSTAL STRUCTURE OF THE T4 REGA TRANSLATIONAL REGULATOR PROTEIN AT 1.9 ANGSTROMS RESOLUTION
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Detector technology | IMAGE PLATE |
Collection date | 1994-08-20 |
Detector | MARRESEARCH |
Wavelength(s) | 1.1 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 82.708, 85.725, 43.485 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 7.000 - 1.900 |
R-factor | 0.18 |
Rwork | 0.180 |
R-free | 0.21400 |
RMSD bond length | 0.015 |
RMSD bond angle | 3.250 |
Phasing software | X-PLOR (3.0) |
Refinement software | X-PLOR (3.0) |
Data quality characteristics
Overall | |
High resolution limit [Å] | 1.900 * |
Rmerge | 0.045 |
Number of reflections | 18037 |
Completeness [%] | 74.0 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 8.5 * | ||
1 | unknown * | 8.5 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 3 (mg/ml) | |
2 | 1 | drop | PEG4000 | 12.5 (%(w/v)) | |
3 | 1 | drop | 0.01 (M) | ||
4 | 1 | drop | Tris-HCl | 0.05 (M) | |
5 | 1 | reservoir | salt | twice the concentration | |
6 | 1 | reservoir | PEG4000 | 25 (%(w/v)) |