2IDG
Crystal Structure of hypothetical protein AF0160 from Archaeoglobus fulgidus
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-08-17 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.97911 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 65.187, 69.744, 133.978 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.830 - 2.690 |
R-factor | 0.24701 |
Rwork | 0.244 |
R-free | 0.29677 |
Structure solution method | SAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.361 |
Data reduction software | HKL-2000 |
Data scaling software | SCALEPACK |
Phasing software | SCA2STRUCTURE |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.800 |
High resolution limit [Å] | 2.690 | 2.690 |
Number of reflections | 18724 | |
<I/σ(I)> | 28.75 | 4.12 |
Completeness [%] | 97.0 | 89 |
Redundancy | 11.9 | 6.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.9 | 291 | SITTING DROP MODIFIED MICROBATCH USING 0.5 MICROLITER DROPS CONTAINING EQUAL VOLUMES OF PROTEIN CONCENTRATE (40 mg/ml) AND RESERVOIR SOLUTION CONTAINING 30% PEG 3350, 0.15M NASCN, 0.01M SPERMINE-HCL, pH 6.9, VAPOR DIFFUSION, SITTING DROP, temperature 291K |