3MTG
Crystal structure of human S-adenosyl homocysteine hydrolase-like 1 protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | BESSY BEAMLINE 14.2 |
| Synchrotron site | BESSY |
| Beamline | 14.2 |
| Temperature [K] | 77 |
| Detector technology | CCD |
| Collection date | 2009-11-26 |
| Detector | MX-225 |
| Wavelength(s) | 0.91841 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 186.240, 68.600, 90.370 |
| Unit cell angles | 90.00, 115.27, 90.00 |
Refinement procedure
| Resolution | 33.590 - 2.640 |
| R-factor | 0.2042 |
| Rwork | 0.203 |
| R-free | 0.24900 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3gvp |
| RMSD bond length | 0.010 |
| RMSD bond angle | 1.150 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | BALBES |
| Refinement software | BUSTER (2.9.2) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 46.625 | 2.780 |
| High resolution limit [Å] | 2.640 | 2.640 |
| Rmerge | 0.070 | 0.414 |
| Number of reflections | 30565 | |
| Redundancy | 7.7 | 7.7 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8.5 | 277 | 0.2 M tri-sodium citrate dehydrate, 18% PEG 3350,0.1 M CHES, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
