2IS5
Crystal structure of 3 residues truncated version of protein NMB1012 from Neisseria meningitides
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-ID |
Synchrotron site | APS |
Beamline | 19-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2006-07-13 |
Detector | ADSC QUANTUM 315 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 65.744, 79.789, 65.605 |
Unit cell angles | 90.00, 105.40, 90.00 |
Refinement procedure
Resolution | 39.800 - 1.850 |
R-factor | 0.1983 |
Rwork | 0.197 |
R-free | 0.22877 |
Structure solution method | SAD |
RMSD bond length | 0.016 |
RMSD bond angle | 1.436 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 1.870 |
High resolution limit [Å] | 1.850 | 1.850 |
Rmerge | 0.075 | 0.475 |
Number of reflections | 55262 | |
<I/σ(I)> | 46.8 | 4.32 |
Completeness [%] | 99.7 | 100 |
Redundancy | 7.2 | 6.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 289 | 20 % PEG 3000, Citrate, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 289K |