3L0G
Crystal structure of Nicotinate-nucleotide pyrophosphorylase from Ehrlichia chaffeensis at 2.05A resolution
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | ALS BEAMLINE 5.0.1 |
| Synchrotron site | ALS |
| Beamline | 5.0.1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2009-11-07 |
| Detector | ADSC QUANTUM 210r |
| Wavelength(s) | 0.9774 |
| Spacegroup name | P 1 |
| Unit cell lengths | 60.530, 77.320, 78.320 |
| Unit cell angles | 113.01, 91.82, 111.68 |
Refinement procedure
| Resolution | 50.000 - 2.050 |
| R-factor | 0.177 |
| Rwork | 0.174 |
| R-free | 0.22600 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | pdb deposition 3GNN modified with CCP4 program CHAINSAW |
| RMSD bond length | 0.015 |
| RMSD bond angle | 1.454 |
| Data reduction software | XDS |
| Data scaling software | XSCALE |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.100 |
| High resolution limit [Å] | 2.050 | 2.050 |
| Rmerge | 0.087 | 0.420 |
| Number of reflections | 72223 | |
| <I/σ(I)> | 10.27 | 2.4 |
| Completeness [%] | 96.6 | 95.4 |
| Redundancy | 2.3 | 2.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 290 | MD PACT SCREEN E6: 20% PEG 3350, 200MM NA-FORMATE; EHCHA.01074.A AT 29MG/ML, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 290K |
