1NAA
Cellobiose Dehydrogenase Flavoprotein Fragment in Complex with Cellobionolactam
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-02-06 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.977 |
| Spacegroup name | H 3 |
| Unit cell lengths | 185.952, 185.952, 81.438 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 30.000 - 1.800 |
| R-factor | 0.146 |
| Rwork | 0.146 |
| R-free | 0.18500 |
| Structure solution method | FOURIER SYNTHESIS |
| Starting model (for MR) | 1kdg |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.920 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | CNS |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 57.000 | 1.900 |
| High resolution limit [Å] | 1.800 | 1.800 |
| Rmerge | 0.089 | 0.498 |
| Total number of observations | 376799 * | |
| Number of reflections | 95043 | |
| <I/σ(I)> | 6.7 | 1.5 |
| Completeness [%] | 97.6 | 85.4 |
| Redundancy | 4 | 2.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 15 * | Hallberg, B.M., (2002) J.Mol.Biol., 315, 421. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 2 (mg/ml) | |
| 2 | 1 | reservoir | ammonium sulfate | 1.6 (M) | |
| 3 | 1 | reservoir | dioxane | 10 (%(v/v)) | |
| 4 | 1 | reservoir | MES | 100 (mM) | pH6.5 |
