1SD0
Structure of arginine kinase C271A mutant
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 17-ID |
Synchrotron site | APS |
Beamline | 17-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-08-01 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 1.15 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.905, 71.255, 79.980 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 2.300 |
R-factor | 0.21 |
Rwork | 0.209 |
R-free | 0.23600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1m15 |
RMSD bond length | 0.007 |
RMSD bond angle | 1.266 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 100.000 | 2.350 |
High resolution limit [Å] | 2.270 | 2.270 |
Rmerge | 0.075 | 0.192 |
Number of reflections | 15669 | |
<I/σ(I)> | 9.3 | 5.1 |
Completeness [%] | 93.3 | 98.9 |
Redundancy | 3.3 | 3.45 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 278 | PEG 6000, magnesium chloride, HEPES, L-arginine, ADP, sodium nitrate, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 278K |