1PCZ
STRUCTURE OF TATA-BINDING PROTEIN
Experimental procedure
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X25 |
| Synchrotron site | NSLS |
| Beamline | X25 |
| Temperature [K] | 173 |
| Detector technology | IMAGE PLATE |
| Collection date | 1994-10-04 |
| Detector | FUJI |
| Spacegroup name | P 61 |
| Unit cell lengths | 89.620, 89.620, 141.280 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 6.000 - 2.200 |
| R-factor | 0.218 |
| Rwork | 0.218 |
| R-free | 0.30100 * |
| Structure solution method | MULTIPLE ISOMORPHOUS REPLACEMENT |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.850 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | SHELXL-96 |
| Refinement software | X-PLOR (3.843) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.330 |
| High resolution limit [Å] | 2.100 | 2.200 |
| Rmerge | 0.079 | 0.237 |
| Number of reflections | 36912 | |
| <I/σ(I)> | 16.9 | 4.5 |
| Completeness [%] | 98.8 | 98.6 |
| Redundancy | 3.2 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 7.5 | 18 * | 50% SATURATED AMMONIUM SULFATE, 0.1 M TRIS PH 7.5, 0.1 M KCL |
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 | 100 (mM) | |
| 3 | 1 | drop | 100 (mM) | ||
| 4 | 1 | drop | ammonium sulfate | 25 (%sat) | |
| 5 | 1 | reservoir | Tris-HCl | 100 (mM) | |
| 6 | 1 | reservoir | 100 (mM) | ||
| 7 | 1 | reservoir | ammonium sulfate | 50 (%sat) |
