5KLY
Human Histidine Triad Nucleotide Binding Protein 1 (hHint1) H112N mutant adenosine nucleoside phosphoramidate substrate 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 | 77.865, 46.502, 64.063 |
Unit cell angles | 90.00, 94.80, 90.00 |
Refinement procedure
Resolution | 63.838 - 1.300 |
R-factor | 0.1496 |
Rwork | 0.148 |
R-free | 0.17110 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 3tw2 |
RMSD bond length | 0.005 |
RMSD bond angle | 0.966 |
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] | 63.840 | 63.840 | 1.320 |
High resolution limit [Å] | 1.300 | 7.120 | 1.300 |
Rmerge | 0.049 | 0.022 | 0.262 |
Rmeas | 0.058 | ||
Rpim | 0.030 | ||
Total number of observations | 195307 | ||
Number of reflections | 53994 | ||
<I/σ(I)> | 19 | ||
Completeness [%] | 96.0 | 89.5 | 93.8 |
Redundancy | 3.6 | 3.4 | 3.5 |
CC(1/2) | 0.999 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.4 | 293 | 100 mM MES, 32% PEG 8000 |