2VUN
The Crystal Structure of Enamidase at 1.9 A Resolution - A new Member of the Amidohydrolase Superfamily
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | MPG/DESY, HAMBURG BEAMLINE BW6 |
Synchrotron site | MPG/DESY, HAMBURG |
Beamline | BW6 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-01-01 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 146.352, 159.824, 161.683 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 107.830 - 1.890 |
R-factor | 0.176 |
Rwork | 0.176 |
R-free | 0.19800 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.008 |
RMSD bond angle | 1.097 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 39.000 | 1.940 |
High resolution limit [Å] | 1.890 | 1.890 |
Rmerge | 0.040 | 0.250 |
Number of reflections | 148870 | |
<I/σ(I)> | 18.5 | 2.9 |
Completeness [%] | 99.0 | 91 |
Redundancy | 3.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 7 | 0.1 M TRIS/HCL PH 7.0, 17.5 W/V-% PEG8000, 0.2 M AMMONIUM SULFATE |