2BP1
Structure of the aflatoxin aldehyde reductase in complex with NADPH
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 | 2005-03-13 |
Detector | MARRESEARCH |
Spacegroup name | P 1 |
Unit cell lengths | 58.989, 78.786, 86.019 |
Unit cell angles | 88.72, 71.14, 75.22 |
Refinement procedure
Resolution | 40.000 - 2.400 |
R-factor | 0.157 |
Rwork | 0.155 |
R-free | 0.20500 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1gve |
RMSD bond length | 0.013 |
RMSD bond angle | 1.402 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.980 | 2.500 |
High resolution limit [Å] | 2.400 | 2.400 |
Rmerge | 0.080 | 0.250 |
Number of reflections | 49989 | |
<I/σ(I)> | 6.4 | 1.9 |
Completeness [%] | 91.0 | 60 |
Redundancy | 1.62 | 0.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | SITTING DROP RESERVOIR: 0.2 M AMMONIUM CITRATE 20 % PEG3350 PROTEIN: 0.01 M HEPES PH 7.5 0.5 M NACL 5 % GLYCEROL 0.5 % TCEP |