3NFY
The Structure of Human Bisphosphoglycerate Mutase to 1.94A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ESRF BEAMLINE ID14-4 |
| Synchrotron site | ESRF |
| Beamline | ID14-4 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-09-03 |
| Detector | ADSC QUANTUM 315r |
| Wavelength(s) | 1.4 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 38.472, 61.345, 122.696 |
| Unit cell angles | 90.00, 95.87, 90.00 |
Refinement procedure
| Resolution | 54.810 - 1.940 |
| R-factor | 0.183 |
| Rwork | 0.178 |
| R-free | 0.27700 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1T8P.pdb |
| RMSD bond length | 0.022 |
| RMSD bond angle | 1.882 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA (3.2.17) |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 122.169 | 54.830 | 2.040 |
| High resolution limit [Å] | 1.940 | 6.130 | 1.940 |
| Rmerge | 0.062 | 0.032 | 0.281 |
| Total number of observations | 5016 | 17704 | |
| Number of reflections | 40132 | ||
| <I/σ(I)> | 15.4 | 16.5 | 2 |
| Completeness [%] | 95.0 | 98.8 | 84.9 |
| Redundancy | 3.6 | 3.6 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7 | 290 | 20% PEG 6K, 100mM Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 290K |
