1VMK
Crystal structure of Purine nucleoside phosphorylase (TM1596) from Thermotoga maritima at 2.01 A resolution
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-02-20 |
Detector | APS |
Spacegroup name | P 1 |
Unit cell lengths | 46.478, 74.601, 74.591 |
Unit cell angles | 117.34, 100.95, 100.71 |
Refinement procedure
Resolution | 43.340 - 2.010 |
R-factor | 0.20575 |
Rwork | 0.204 |
R-free | 0.23995 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1a9o |
RMSD bond length | 0.017 |
RMSD bond angle | 1.615 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 43.340 | 2.070 |
High resolution limit [Å] | 2.000 | 2.000 |
Number of reflections | 54061 | |
<I/σ(I)> | 12.88 | 2.58 |
Completeness [%] | 97.7 | 93.79 |
Redundancy | 3.77 | 3.43 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION,SITTING DROP,NANODROP | 6.5 | 277 | 0.2M MgCl2, 20.0% PEG-1000, 0.1M Cacodylate pH 6.5, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K |