3CSM
STRUCTURE OF YEAST CHORISMATE MUTASE WITH BOUND TRP AND AN ENDOOXABICYCLIC INHIBITOR
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | ELLIOTT GX-13 |
| Temperature [K] | 123 |
| Detector technology | AREA DETECTOR |
| Collection date | 1996-10-15 |
| Detector | SIEMENS-NICOLET X100 |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 203.500, 203.500, 128.700 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 15.000 - 3.000 |
| R-factor | 0.204 |
| Rwork | 0.204 |
| R-free | 0.24700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1csm |
| RMSD bond length | 0.013 |
| RMSD bond angle | 19.000 * |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | X-PLOR (3.851) |
| Refinement software | X-PLOR (3.851) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.200 |
| High resolution limit [Å] | 3.000 | 3.000 |
| Rmerge | 0.092 | 0.325 |
| Total number of observations | 51388 * | |
| Number of reflections | 20253 | |
| Completeness [%] | 98.4 | 99.1 |
| Redundancy | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 8 | HANGING DROP, 19 % (W/V) PEG MONOMETHYLETHER 5000, 5 MM DTT, 0.15 M TRIS PH 8.0, 0.15 M SODIUM ACETATE, 16 MM TRYPTOPHAN, 3 MM INHIBITOR, 10 MG/ML PROTEIN, vapor diffusion - hanging drop |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | drop | endo-oxabicyclic inhibitor | 3 (mM) | |
| 3 | 1 | reservoir | mPEG5000 | 19 (%(w/v)) | |
| 4 | 1 | reservoir | dithiothreitol | 5 (mM) | |
| 5 | 1 | reservoir | Tris-HCl | 0.15 (M) | |
| 6 | 1 | reservoir | sodium acetate | 0.15 (M) | |
| 7 | 1 | reservoir | tryptophan | 16 (mM) |
