2BLE
Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP
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 | 2005-02-09 |
Detector | MARMOSAIC 225 mm CCD |
Spacegroup name | P 4 21 2 |
Unit cell lengths | 117.780, 117.780, 54.420 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.000 - 1.900 |
R-factor | 0.18 |
Rwork | 0.177 |
R-free | 0.22800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1eep |
RMSD bond length | 0.017 |
RMSD bond angle | 1.663 |
Data reduction software | XDS |
Data scaling software | XDS |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.000 |
High resolution limit [Å] | 1.900 | 1.900 |
Rmerge | 0.120 | 0.460 |
Number of reflections | 27431 | |
<I/σ(I)> | 27.1 | 2.11 |
Completeness [%] | 89.1 | 78.7 |
Redundancy | 7.6 | 4.04 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.5 | 0.1 NA-CACODYLATE PH=6.5 17% PEG10K 0.2 M CA-ACETATE 25% GLYCEROL, pH 6.50 |