2QYG
Crystal Structure of a RuBisCO-like Protein rlp2 from Rhodopseudomonas palustris
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.2 |
Synchrotron site | ALS |
Beamline | 8.2.2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-11-22 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.9537 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 68.662, 119.529, 203.040 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 77.380 - 3.300 |
R-factor | 0.20402 |
Rwork | 0.203 |
R-free | 0.23228 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1ykw |
RMSD bond length | 0.012 |
RMSD bond angle | 1.396 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 90.000 | 3.420 |
High resolution limit [Å] | 3.300 | 3.300 |
Number of reflections | 26399 | |
<I/σ(I)> | 9.6 | 3.8 |
Completeness [%] | 99.7 | 99.5 |
Redundancy | 6.2 | 5.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.6 | 293 | 280mM ammonium acetate, 100mM sodium acetate, 30% PEG4000, pH 4.6, VAPOR DIFFUSION, SITTING DROP, temperature 293K |