1MEJ
Human Glycinamide Ribonucleotide Transformylase domain at pH 8.5
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2001-06-20 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9706 |
Spacegroup name | H 3 2 |
Unit cell lengths | 152.510, 152.510, 193.390 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 30.000 * - 2.000 |
Rwork | 0.216 |
R-free | 0.25200 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1c2t |
RMSD bond length | 0.009 |
RMSD bond angle | 1.340 * |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 * | 2.100 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.060 | 0.372 |
Total number of observations | 118898 * | |
Number of reflections | 53638 | |
<I/σ(I)> | 1.6 | |
Completeness [%] | 97.8 * | 96.8 * |
Redundancy | 2.21 * | 1.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 4 * | PEG4000, PEG400, NaCl, Tris pH 8.5,, 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 |