2O4T
CRYSTAL STRUCTURE OF a protein of the DUF1048 family with a left-handed superhelix fold (BH3976) FROM BACILLUS HALODURANS AT 1.95 A RESOLUTION
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-D |
| Synchrotron site | APS |
| Beamline | 23-ID-D |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-10-19 |
| Detector | MARMOSAIC 300 mm CCD |
| Spacegroup name | H 3 2 |
| Unit cell lengths | 85.577, 85.577, 104.575 |
| Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
| Resolution | 60.412 - 1.950 |
| R-factor | 0.205 |
| Rwork | 0.203 |
| R-free | 0.25500 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb enrty 2o3l |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.442 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 60.412 | 60.470 | 2.000 |
| High resolution limit [Å] | 1.950 | 8.720 | 1.950 |
| Rmerge | 0.091 | 0.069 | 0.521 |
| Total number of observations | 606 | 2463 | |
| Number of reflections | 10900 | ||
| <I/σ(I)> | 4.1 | 8.6 | 1.4 |
| Completeness [%] | 99.8 | 98.6 | 98.9 |
| Redundancy | 5.1 | 4.4 | 3.2 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP, NANODROP | 4.2 | 277 | 0.2M (NH4)2SO4, 10.0% Glycerol, 20.0% PEG-300, 0.1M Phosphate Citrate pH 4.2, VAPOR DIFFUSION, SITTING DROP, NANODROP, temperature 277K |
