3FWY
Crystal structure of the L protein of Rhodobacter sphaeroides light-independent protochlorophyllide reductase (BchL) with MgADP bound: a homologue of the nitrogenase Fe protein
Replaces: 3ENDExperimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2008-01-19 |
Detector | MARMOSAIC 325 mm CCD |
Wavelength(s) | 0.98000 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 56.729, 86.622, 117.169 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 33.020 - 1.630 |
R-factor | 0.17529 |
Rwork | 0.174 |
R-free | 0.19860 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2nip |
RMSD bond length | 0.008 |
RMSD bond angle | 1.206 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.670 |
High resolution limit [Å] | 1.630 | 1.630 |
Number of reflections | 133747 | |
<I/σ(I)> | 40 | 4.6 |
Completeness [%] | 96.4 | 93.83 |
Redundancy | 2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | CAPILLARY BATCH DIFFUSION | 7.8 | 301 | 20-25% PEG 3350, 200mM Magnesium formate, 10mM MgADP, pH 7.8, CAPILLARY BATCH DIFFUSION, temperature 301K |