3PRU
Crystal Structure of Phycobilisome 32.1 kDa linker polypeptide, phycocyanin-associated, rod 1 (fragment 14-158) from Synechocystis sp. PCC 6803, Northeast Structural Genomics Consortium Target SgR182A
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSLS BEAMLINE X4A |
| Synchrotron site | NSLS |
| Beamline | X4A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2010-11-02 |
| Detector | ADSC QUANTUM 4 |
| Wavelength(s) | 0.979 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 74.354, 91.532, 124.673 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 47.770 - 2.677 |
| R-factor | 0.195 |
| Rwork | 0.193 |
| R-free | 0.24100 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 3ohw |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.172 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | BALBES |
| Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 2.800 |
| High resolution limit [Å] | 2.700 | 2.700 |
| Rmerge | 0.101 | 0.512 |
| Number of reflections | 45882 | |
| <I/σ(I)> | 26.2 | 4.7 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 4.8 | 4.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 293 | Protein solution: 100mM NaCl, 5mM DTT, 0.02% NaN3, 10mM Tris-HCl (pH 7.5). Reservoir solution: 3.7M NaCl, 0.1M HEPES-Na, VAPOR DIFFUSION, HANGING DROP, temperature 293KK |






