1OLQ
The Trichoderma reesei cel12a P201C mutant, structure at 1.7 A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-1 |
| Synchrotron site | ESRF |
| Beamline | ID14-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2000-12-03 |
| Detector | MARRESEARCH |
| Spacegroup name | P 31 |
| Unit cell lengths | 70.616, 70.616, 69.092 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 20.000 - 1.700 |
| R-factor | 0.21035 |
| Rwork | 0.209 |
| R-free | 0.25100 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h8v |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.700 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.730 |
| High resolution limit [Å] | 1.700 | 1.700 |
| Rmerge | 0.074 | 0.390 |
| Total number of observations | 184371 * | |
| Number of reflections | 42832 * | |
| <I/σ(I)> | 18.3 | 2.8 |
| Completeness [%] | 99.8 * | 99.6 * |
| Redundancy | 4.3 | 99.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6 | 20-24 * | pH 6.00 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | reservoir | cacodylate | 0.02 (M) | pH6.0 |
| 2 | 1 | reservoir | calcium acetate | 0.02 (M) | |
| 3 | 1 | reservoir | PEG2000 MME | 10-30 (%(w/w)) | |
| 4 | 1 | drop | protein | 20 (mg/ml) |
