1G9G
XTAL-STRUCTURE OF THE FREE NATIVE CELLULASE CEL48F
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 290 |
Detector technology | IMAGE PLATE |
Collection date | 1999-08-30 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9796 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 61.530, 84.770, 122.120 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 * - 1.850* |
R-factor | 0.165 |
Rwork | 0.165 |
R-free | 0.19500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fce |
RMSD bond length | 0.005 |
RMSD bond angle | 22.100 * |
Data reduction software | DENZO |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 1.900 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.091 | 0.354 |
Number of reflections | 49813 | |
<I/σ(I)> | 6.8 | 1.9 |
Completeness [%] | 98.2 | 88.9 |
Redundancy | 3.8 | 2.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 * | Reverbel-Leroy, C., (1997) Acta Crystallogr., D.54, 114. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 20 (mg/ml) | |
2 | 1 | drop | IG4 | 2 (mM) | |
3 | 1 | reservoir | 0.5 (M) | or 0.3M | |
4 | 1 | drop | PEG4000 |