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 |
