1E2W
N168F mutant of cytochrome f from Chlamydomonas reinhardtii
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 19-ID |
| Synchrotron site | APS |
| Beamline | 19-ID |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 1999-04-15 |
| Detector | CUSTOM-MADE |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 59.030, 81.180, 61.080 |
| Unit cell angles | 90.00, 103.52, 90.00 |
Refinement procedure
| Resolution | 27.410 - 1.600 |
| R-factor | 0.197 |
| Rwork | 0.197 |
| R-free | 0.22600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1e2v |
| RMSD bond length | 0.005 |
| RMSD bond angle | 25.900 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | CNS (1.0) |
| Refinement software | CNS (1.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 27.840 | 1.660 |
| High resolution limit [Å] | 1.600 | 1.600 |
| Rmerge | 0.046 | 0.378 |
| Total number of observations | 277890 * | |
| Number of reflections | 73580 | |
| <I/σ(I)> | 28.6 | 3.54 |
| Completeness [%] | 99.6 | 100 |
| Redundancy | 3.8 | 3.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion * | 7.5 * | THE PROTEIN WAS BUFFERED IN 10 MM NA2HPO4/NAH2PO4, PH 7.5, 1 MM DTT, THE RESERVOIR CONTAINED 100 MM MES, PH 6.7, 200 MM AMMONIUM FORMATE, 14% GLYCEROL, 17% PEG-3350. |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | dithiothreitol | 1 (mM) | |
| 3 | 1 | reservoir | MES | 100 (mM) | |
| 4 | 1 | reservoir | ammonium formate | 200 (mM) | |
| 5 | 1 | reservoir | glycerol | 14 (%) | |
| 6 | 1 | reservoir | PEG3350 | 17 (%) |
