5KM3
Human Histidine Triad Nucleotide Binding Protein 1 (hHint1) UMP catalytic product complex
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 4.2.2 |
Synchrotron site | ALS |
Beamline | 4.2.2 |
Temperature [K] | 100 |
Detector technology | CMOS |
Collection date | 2015-09-24 |
Detector | RDI CMOS_8M |
Wavelength(s) | 1.000 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 78.133, 46.305, 63.862 |
Unit cell angles | 90.00, 94.44, 90.00 |
Refinement procedure
Resolution | 63.671 - 1.200 |
R-factor | 0.1646 |
Rwork | 0.164 |
R-free | 0.18060 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3tw2 |
RMSD bond length | 0.006 |
RMSD bond angle | 1.183 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.9) |
Phasing software | PHASER (2.6.0) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 63.671 | 63.670 | 1.220 |
High resolution limit [Å] | 1.200 | 6.570 | 1.200 |
Rmerge | 0.047 | 0.020 | 0.358 |
Number of reflections | 70340 | ||
<I/σ(I)> | 17.4 | ||
Completeness [%] | 98.9 | 89.5 | 89.8 |
Redundancy | 3.4 | 3.3 | 2.4 |
CC(1/2) | 0.999 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.1 | 293 | 100 mM MES, 38% PEG 8000, |