1DT5
THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE BM14 |
| Synchrotron site | ESRF |
| Beamline | BM14 |
| Temperature [K] | 110 |
| Detector technology | IMAGE PLATE |
| Collection date | 1998-01-01 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 85.435, 162.878, 86.717 |
| Unit cell angles | 90.00, 98.45, 90.00 |
Refinement procedure
| Resolution | 20.000 - 2.400 |
| Rwork | 0.244 |
| R-free | 0.31500 |
| RMSD bond length | 0.009 |
| RMSD bond angle | 0.030 |
| 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 | 2.440 |
| High resolution limit [Å] | 2.400 | 2.400 |
| Rmerge | 0.062 | 0.424 * |
| Number of reflections | 91415 | |
| <I/σ(I)> | 15.8 | |
| Completeness [%] | 98.4 | 98.6 |
| Redundancy | 2.75 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | unknown * | 8 * | PEG 5000, magnesium chloride, C8E5, pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 110K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 5 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | reservoir | Tris-HCl | 0.1 (M) | |
| 4 | 1 | reservoir | 25 (mM) | ||
| 5 | 1 | reservoir | mPEG5000 | 15-17 (%(w/v)) | |
| 6 | 1 | reservoir | C8E3 | 0.5 (%(v/v)) | |
| 7 | 1 | reservoir | ethylene glycol | 20 (%(v/v)) |
