1XNF
Crystal structure of E.coli TPR-protein NlpI
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-11-18 |
Detector | CUSTOM-MADE |
Wavelength(s) | 0.9785, 0.9795, 0.9500 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 64.351, 81.654, 136.660 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 39.840 - 1.980 |
R-factor | 0.17122 |
Rwork | 0.169 |
R-free | 0.20577 |
Structure solution method | MAD |
RMSD bond length | 0.023 |
RMSD bond angle | 1.854 |
Data reduction software | HKL-2000 |
Data scaling software | CCP4 ((TRUNCATE)) |
Phasing software | SOLVE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 40.000 | 2.100 |
High resolution limit [Å] | 1.980 | 1.980 |
Rmerge | 0.049 | 0.355 |
Number of reflections | 48199 | |
<I/σ(I)> | 40.4 | 4.8 |
Completeness [%] | 83.6 | |
Redundancy | 5.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 295 | HEPES, MgCl2, PEG400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 295K |