1OLR
The Humicola grisea Cel12A Enzyme Structure at 1.2 A Resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | MAX II BEAMLINE I711 |
| Synchrotron site | MAX II |
| Beamline | I711 |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-04-25 |
| Detector | MARRESEARCH |
| Spacegroup name | P 43 21 2 |
| Unit cell lengths | 49.231, 49.231, 165.517 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 30.000 - 1.220 * |
| R-factor | 0.13508 |
| Rwork | 0.135 |
| R-free | 0.15100 * |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1h8v |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.600 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 1.240 |
| High resolution limit [Å] | 1.220 | 1.220 |
| Rmerge | 0.076 | 0.352 * |
| Total number of observations | 321815 * | |
| Number of reflections | 58847 | |
| <I/σ(I)> | 24 | 4 |
| Completeness [%] | 94.6 * | 84.4 * |
| Redundancy | 5.5 |
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) |
