1T8P
Crystal structure of Human erythrocyte 2,3-bisphosphoglycerate 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 | 2003-10-26 |
Detector | MARRESEARCH |
Wavelength(s) | 0.9 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 38.638, 61.768, 123.333 |
Unit cell angles | 90.00, 94.99, 90.00 |
Refinement procedure
Resolution | 29.950 - 2.500 |
R-factor | 0.2 |
Rwork | 0.200 |
R-free | 0.26600 |
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] | 50.000 | 2.560 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 18907 | |
Completeness [%] | 96.0 | 97.2 |
Redundancy | 9.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 291 | 20%(w/v) PEG6000, 0.1M Hepes, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 291K |