2H63
Crystal Structure of Human Biliverdin Reductase A
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-03-04 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9789 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 90.787, 92.747, 147.755 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 50.000 - 2.700 |
R-factor | 0.23943 |
Rwork | 0.237 |
R-free | 0.28691 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1LC0.pdb |
RMSD bond length | 0.014 |
RMSD bond angle | 1.514 |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 41.300 | 2.850 |
High resolution limit [Å] | 2.700 | 2.700 |
Number of reflections | 33769 | |
Completeness [%] | 96.8 | 92.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 277 | MgCl2, Bis-Tris, PEG 3350, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 277K |