3SE5
Fic protein from NEISSERIA MENINGITIDIS mutant delta8 in complex with AMPPNP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X06DA |
Synchrotron site | SLS |
Beamline | X06DA |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-04-14 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 1.0000 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 73.945, 65.031, 75.995 |
Unit cell angles | 90.00, 107.08, 90.00 |
Refinement procedure
Resolution | 15.000 - 1.700 |
R-factor | 0.16 |
Rwork | 0.159 |
R-free | 0.19700 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2g03 |
RMSD bond length | 0.011 |
RMSD bond angle | 1.317 |
Data reduction software | MOSFLM |
Data scaling software | SCALA (CCP4_3.3.16 2010/01/06) |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0109) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 37.030 | 37.030 | 1.790 |
High resolution limit [Å] | 1.700 | 5.380 | 1.700 |
Rmerge | 0.069 | 0.030 | 0.370 |
Total number of observations | 9835 | 36210 | |
Number of reflections | 73865 | ||
<I/σ(I)> | 9.8144 | 20.86 | 1.97 |
Completeness [%] | 97.7 | 98.25 | 95.43 |
Redundancy | 4 | 4.03 | 3.46 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.6 | 293 | 44% w/v PEG 600, 0.1M Na-citrate, pH 5.6, vapor diffusion, hanging drop, temperature 293K |