1BHJ
CRYSTAL STRUCTURE OF APO-GLYCINE N-METHYLTRANSFERASE (GNMT)
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | RIGAKU RUH2R |
| Temperature [K] | 108 |
| Detector technology | IMAGE PLATE |
| Collection date | 1995-06 |
| Detector | RIGAKU |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 85.390, 174.210, 44.710 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 8.000 - 2.500 |
| R-factor | 0.221 |
| Rwork | 0.221 |
| R-free | 0.31800 |
| Structure solution method | RIGID BODY REFINEMENT |
| Starting model (for MR) | 1xva |
| RMSD bond length | 0.007 |
| RMSD bond angle | 27.770 * |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | X-PLOR (3.1) |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.540 |
| High resolution limit [Å] | 2.500 | 2.500 |
| Rmerge | 0.106 * | 0.417 * |
| Total number of observations | 254910 * | |
| Number of reflections | 22481 | |
| <I/σ(I)> | 10.59 | 2.73 |
| Completeness [%] | 93.8 | 87 |
| Redundancy | 2.7 | 2.5 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 6.8 | 11 * | equal volume of protein and reservoir solution were used for the drop * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 8 (mg/ml) | |
| 10 | 1 | reservoir | 100 (mM) | ||
| 2 | 1 | drop | Tris-HCl | 10 (mM) | |
| 3 | 1 | drop | 1 (mM) | ||
| 4 | 1 | drop | beta-mercaptoethanol | 10 (mM) | |
| 5 | 1 | drop | dithiothreitol | 2 (mM) | |
| 6 | 1 | drop | EDTA | 2 (mM) | |
| 7 | 1 | reservoir | sodium citrate | 0.1 (M) | |
| 8 | 1 | reservoir | ammonium phosphate | 1 (M) | |
| 9 | 1 | reservoir | glycerol | 5 (%) |
