3VNS
Co-crystal structure of NRPS adenylation protein CytC1 with D-valine and AMP from streptomyces
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL44B2 |
| Synchrotron site | SPring-8 |
| Beamline | BL44B2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-11-22 |
| Detector | ADSC QUANTUM 210 |
| Wavelength(s) | 1.0 |
| Spacegroup name | I 2 3 |
| Unit cell lengths | 156.544, 156.544, 156.544 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 39.136 - 2.001 |
| R-factor | 0.1926 |
| Rwork | 0.191 |
| R-free | 0.21560 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1amu |
| RMSD bond length | 0.005 |
| RMSD bond angle | 1.012 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | PHENIX (1.7_650) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.030 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.062 | 0.461 |
| Number of reflections | 43061 | |
| <I/σ(I)> | 70.394 | 8.185 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 22.6 | 20.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 7.2 | 293 | 0.1M ammonium sulfate, 24-32% PEG5000 monomethyl ether, 1mM ATP, 100mM Hepes buffer, pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K |
