5HMM
Crystal Structure of T5 D15 Protein Co-crystallized with Metal Ions
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | DIAMOND BEAMLINE I03 |
Synchrotron site | Diamond |
Beamline | I03 |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2011-03-01 |
Detector | DECTRIS PILATUS 6M |
Wavelength(s) | 0.97836 |
Spacegroup name | P 1 |
Unit cell lengths | 46.831, 58.591, 59.729 |
Unit cell angles | 66.88, 79.40, 73.78 |
Refinement procedure
Resolution | 38.350 - 1.500 |
R-factor | 0.1501 |
Rwork | 0.148 |
R-free | 0.19670 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1exn |
RMSD bond length | 0.011 |
RMSD bond angle | 1.329 |
Data reduction software | iMOSFLM |
Data scaling software | SCALA (3.3.21) |
Phasing software | PHASER |
Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 54.735 | 38.730 | 1.580 |
High resolution limit [Å] | 1.500 | 4.740 | 1.500 |
Rmerge | 0.039 | 0.322 | |
Rmeas | 0.093 | ||
Rpim | 0.042 | 0.018 | 0.296 |
Total number of observations | 313085 | 15866 | 25799 |
Number of reflections | 83343 | ||
<I/σ(I)> | 10.5 | 38.1 | 2.5 |
Completeness [%] | 93.1 | 97.3 | 90.4 |
Redundancy | 3.8 | 5.7 | 2.2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 280 | PACT H2: 0.2M Na bromide, 0.1M Bis Tris propane pH 8.5, 20% PEG 3350 |