1M5H
Formylmethanofuran:tetrahydromethanopterin formyltransferase from Archaeoglobus fulgidus
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2001-06-20 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.8452 |
| Spacegroup name | P 1 |
| Unit cell lengths | 77.100, 81.810, 99.100 |
| Unit cell angles | 90.10, 110.04, 93.75 |
Refinement procedure
| Resolution | 29.250 - 2.000 |
| R-factor | 0.229 |
| Rwork | 0.229 |
| R-free | 0.28200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | Formylmethanofuran:Tetrahydromethanopterin Formyltransferase from Methanosarcina barkeri |
| RMSD bond length | 0.006 |
| RMSD bond angle | 24.200 * |
| Data reduction software | DENZO |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | EPMR |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.100 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.080 * | 0.223 * |
| Total number of observations | 839340 * | |
| Number of reflections | 150792 | |
| Completeness [%] | 86.0 | 67 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 4 * | Imidazol/Malate, KSCN, PEG 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP at 277K |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 12 (mg/ml) | |
| 2 | 1 | drop | MOPS | 10 (mM) | pH7.0 |
| 3 | 1 | reservoir | imidazole-malate | 0.1 (M) | |
| 4 | 1 | reservoir | KSCN | 0.2 (M) | |
| 5 | 1 | reservoir | PEG3350 | 23 (%) |
