1MEO
human glycinamide ribonucleotide Transformylase at pH 4.2
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2001-11-16 |
| Detector | ADSC QUANTUM 9 |
| Wavelength(s) | 0.976 |
| Spacegroup name | P 65 2 2 |
| Unit cell lengths | 78.130, 78.130, 230.910 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 46.000 * - 1.720 |
| R-factor | 0.226 |
| Rwork | 0.223 |
| R-free | 0.24000 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1mej |
| RMSD bond length | 0.008 * |
| RMSD bond angle | 1.140 * |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.0) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.000 * | 1.780 |
| High resolution limit [Å] | 1.720 | 1.720 |
| Rmerge | 0.072 | 0.418 |
| Total number of observations | 167456 * | |
| Number of reflections | 40379 | |
| <I/σ(I)> | 23.4 | 1.65 |
| Completeness [%] | 98.7 * | 99 |
| Redundancy | 4.15 * | 1.9 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 * | 4 * | 1.9-2.1M Ammonium Sulfate, 100mM Na Acetate pH 4.2-4.6, VAPOR DIFFUSION, SITTING DROP, temperature 282K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 10 (mg/ml) | |
| 2 | 1 | reservoir | PEG4000 | 18-21 (%) | |
| 3 | 1 | reservoir | PEG400 | 2 (%) | |
| 4 | 1 | reservoir | 0.1 (M) | ||
| 5 | 1 | reservoir | Tris | 0.1 (M) | pH8.5 |
