3FGY
CRYSTAL STRUCTURE OF A NTF2-LIKE PROTEIN (BXE_B1094) FROM BURKHOLDERIA XENOVORANS LB400 AT 1.59 A RESOLUTION
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 23-ID-B |
| Synchrotron site | APS |
| Beamline | 23-ID-B |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2008-10-11 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.94645,0.97967 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 45.950, 66.080, 91.000 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.037 - 1.590 |
| R-factor | 0.184 |
| Rwork | 0.183 |
| R-free | 0.21100 |
| Structure solution method | MAD |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.553 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.037 | 29.037 | 1.650 |
| High resolution limit [Å] | 1.590 | 3.420 | 1.590 |
| Rmerge | 0.044 | 0.026 | 0.446 |
| Number of reflections | 37939 | 7206 | 7542 |
| <I/σ(I)> | 14.92 | 48.2 | 1.7 |
| Completeness [%] | 99.0 | 99.2 | 99.4 |
| Redundancy | 4.6 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 10.5 | 277 | 30.0000% PEG-400, 0.1M CAPS pH 10.5, NANODROP, VAPOR DIFFUSION, SITTING DROP, temperature 277K |
