3GNN
Crystal structure of nicotinate-nucleotide pyrophosphorylase from Burkholderi pseudomallei
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 |
Collection date | 2008-06-18 |
Wavelength(s) | 0.97934 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 160.978, 57.414, 66.243 |
Unit cell angles | 90.00, 106.74, 90.00 |
Refinement procedure
Resolution | 39.140 - 2.250 |
R-factor | 0.217 |
Rwork | 0.214 |
R-free | 0.27300 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.020 |
RMSD bond angle | 1.791 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | MOLREP |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.330 |
High resolution limit [Å] | 2.250 | 2.250 |
Rmerge | 0.068 | 0.589 |
Number of reflections | 27262 | |
<I/σ(I)> | 21.998 | 2.27 |
Completeness [%] | 98.9 | 97.7 |
Redundancy | 3.8 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 289 | HAMPTON CRYSTAL SCREEN CONDITION E8, 1.5 M NACL, 10% ETHANOL WITH 25% GLYCEROL AS CRYO-PROTECTANT, 28.7 MG/ML PROTEIN, CRYSTAL ID 109334E8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K |