1FN0
STRUCTURE OF A MUTANT WINGED BEAN CHYMOTRYPSIN INHIBITOR PROTEIN, N14D.
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 | 1998-08-10 |
| Detector | MARRESEARCH |
| Spacegroup name | P 61 2 2 |
| Unit cell lengths | 61.240, 61.240, 210.860 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 10.000 - 2.000 |
| R-factor | 0.209 * |
| Rwork | 0.209 |
| R-free | 0.28700 |
| RMSD bond length | 0.027 * |
| RMSD bond angle | 2.100 * |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 18.000 | 2.000 |
| High resolution limit [Å] | 1.900 | 1.900 |
| Rmerge | 0.087 | 0.423 |
| Total number of observations | 33037 * | |
| Number of reflections | 14503 | |
| <I/σ(I)> | 3.5 | |
| Completeness [%] | 75.7 | 68.8 * |
| Redundancy | 2 | 2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.4 | 4 * | Dattagupta, J.K., (1999) Proteins: Struct., Funct., Genet., 35, 321. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8.6 (mg/ml) | |
| 2 | 1 | drop | Tris-HCl | 71.4 (mM) | |
| 3 | 1 | drop | 286 (mM) | ||
| 4 | 1 | drop | ammonium sulfate | 1.4 (%) | |
| 5 | 1 | drop | sodium acetate | 2.9 (mM) | |
| 6 | 1 | reservoir | ammonium sulfate | 25 (%) | |
| 7 | 1 | reservoir | sodium acetate | 60 (mM) |
