1YFK
Crystal structure of human B type phosphoglycerate mutase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | BSRF BEAMLINE 3W1A |
Synchrotron site | BSRF |
Beamline | 3W1A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-03-31 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 42.861, 65.745, 124.812 |
Unit cell angles | 90.00, 94.36, 90.00 |
Refinement procedure
Resolution | 29.070 - 2.700 |
R-factor | 0.216 |
Rwork | 0.216 |
R-free | 0.25500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5pgm |
RMSD bond length | 0.007 |
RMSD bond angle | 1.300 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.760 |
High resolution limit [Å] | 2.700 | 2.700 |
Rmerge | 0.129 | 0.436 |
Number of reflections | 17981 | |
Completeness [%] | 94.7 | 94.4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.7 | 297 | PEG4000, iso-Propanol, tri-Sodium Citrate dehydrate, (NH4)2SO4, pH 5.7, VAPOR DIFFUSION, HANGING DROP, temperature 297K |