1ZP9
Crystal Structure of full-legnth A.fulgidus Rio1 Serine Kinase bound to ATP and Mn2+ ions.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Detector technology | IMAGE PLATE |
Collection date | 2004-11-05 |
Detector | MARRESEARCH |
Wavelength(s) | 0.96860 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 53.306, 80.373, 121.320 |
Unit cell angles | 90.00, 90.02, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.000 |
R-factor | 0.18067 |
Rwork | 0.177 |
R-free | 0.24880 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ztf |
RMSD bond length | 0.018 |
RMSD bond angle | 1.679 |
Data scaling software | HKL-2000 |
Phasing software | MOLREP |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 30.000 |
High resolution limit [Å] | 2.000 |
Number of reflections | 63199 |
<I/σ(I)> | 11.2 |
Redundancy | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION | 6.3 | 293 | PEG 4000, Ammonium Sulfate, MES, pH 6.3, VAPOR DIFFUSION, temperature 293K |