2BMW
Ferredoxin: NADP+ Reductase Mutant With Thr 155 Replaced By Gly, Ala 160 Replaced By Thr, Leu 263 Replaced By Pro, Arg 264 Replaced By Pro and Gly 265 Replaced by Pro (T155G-A160T-L263P-R264P-G265P)
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM16 |
Synchrotron site | ESRF |
Beamline | BM16 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2004-10-02 |
Detector | MARRESEARCH |
Spacegroup name | P 65 |
Unit cell lengths | 85.970, 85.970, 96.250 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 28.140 - 1.500 |
R-factor | 0.185 |
Rwork | 0.185 |
R-free | 0.20700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1que |
RMSD bond length | 0.010 |
RMSD bond angle | 1.500 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.500 | 1.580 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.100 | 0.320 |
Number of reflections | 64511 | |
<I/σ(I)> | 14.5 | 5.3 |
Completeness [%] | 99.9 | 99.7 |
Redundancy | 8.9 | 8.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 5 | pH 5.00 |