2Q7S
Crystal structure of N-formylglutamate amidohydrolase (YP_297560.1) from Ralstonia eutropha JMP134 at 2.00 A resolution
Experimental procedure
| Experimental method | MAD |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL11-1 |
| Synchrotron site | SSRL |
| Beamline | BL11-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2007-05-03 |
| Detector | MARMOSAIC 325 mm CCD |
| Wavelength(s) | 0.91837, 0.97944, 0.97917 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 58.610, 74.835, 145.163 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 29.604 - 2.000 |
| R-factor | 0.202 |
| Rwork | 0.199 |
| R-free | 0.24600 |
| Structure solution method | MAD |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.604 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | SHELX |
| Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 29.604 | 29.600 | 2.050 |
| High resolution limit [Å] | 2.000 | 8.940 | 2.000 |
| Rmerge | 0.078 | 0.043 | 0.382 |
| Total number of observations | 1610 | 11021 | |
| Number of reflections | 43945 | ||
| <I/σ(I)> | 6.9 | 13.5 | 2 |
| Completeness [%] | 99.9 | 93.5 | 99.9 |
| Redundancy | 3.5 | 3 | 3.4 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 6 | 277 | NANODROP, 30.0% PEG 6000, 0.1M MES pH 6.0, VAPOR DIFFUSION, SITTING DROP, temperature 277K |






