1QU4
CRYSTAL STRUCTURE OF TRYPANOSOMA BRUCEI ORNITHINE DECARBOXYLASE
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X12C |
| Synchrotron site | NSLS |
| Beamline | X12C |
| Temperature [K] | 90 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 66.800, 151.700, 85.350 |
| Unit cell angles | 90.00, 102.30, 90.00 |
Refinement procedure
| Resolution | 8.000 * - 2.900 |
| R-factor | 0.23 * |
| Rwork | 0.245 |
| R-free | 0.26800 |
| RMSD bond length | 0.013 |
| RMSD bond angle | 0.039 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | AMoRE |
| Refinement software | REFMAC |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 3.000 |
| High resolution limit [Å] | 2.900 | 2.900 |
| Rmerge | 0.080 | 0.140 |
| Total number of observations | 120960 * | |
| Number of reflections | 36421 | |
| <I/σ(I)> | 14.3 | |
| Completeness [%] | 98.6 | 75.3 |
| Redundancy | 3.3 | 3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 8 * | 289 | Grishin, N.V., (1996) Proteins Struct. Funct. Genet., 24, 272. * |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | PEG3350 | 20 (%) | |
| 2 | 1 | drop | Tris-HCl | 0.1 (M) | |
| 3 | 1 | drop | ammonium acetate | 0.2 (M) | |
| 4 | 1 | drop | dithiothreitol | 10 (mM) | |
| 5 | 1 | drop | protain | 20 (mg/ml) |
