4Q52
2.60 Angstrom resolution crystal structure of a conserved uncharacterized protein from Chitinophaga pinensis DSM 2588
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-F |
| Synchrotron site | APS |
| Beamline | 21-ID-F |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2014-02-03 |
| Detector | MARMOSAIC 225 mm CCD |
| Wavelength(s) | 0.97872 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 51.712, 85.549, 88.195 |
| Unit cell angles | 90.00, 104.19, 90.00 |
Refinement procedure
| Resolution | 29.190 - 2.600 |
| R-factor | 0.17114 |
| Rwork | 0.169 |
| R-free | 0.21529 |
| Structure solution method | SAD |
| RMSD bond length | 0.014 |
| RMSD bond angle | 1.620 |
| Data reduction software | HKL-3000 |
| Data scaling software | HKL-3000 |
| Phasing software | HKL-3000 |
| Refinement software | REFMAC (5.7.0029) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 30.000 | 2.640 |
| High resolution limit [Å] | 2.600 | 2.600 |
| Rmerge | 0.152 | 0.641 |
| Number of reflections | 22847 | |
| <I/σ(I)> | 12.2 | 2.5 |
| Completeness [%] | 99.9 | 100 |
| Redundancy | 4.8 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7 | 295 | protein: 7.8 mg/mL in 10 mM Tris/HCl, 500 mM NaCl, 5 mM BME crystallization: the PACT Suite (C11: 0.2 M CaCl2, 0.1 M HEPES pH 7.0, 20 % (w/v) PEG 6000) cryo: 25 % glucose, VAPOR DIFFUSION, SITTING DROP, temperature 295K |
