5JNV
Crystal structure of bovine low molecular weight protein tyrosine phosphatase (LMPTP) mutant (W49Y N50E) complexed with HEPES
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-2 |
Synchrotron site | SSRL |
Beamline | BL9-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2014-09-14 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0 |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 59.944, 122.939, 44.888 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.250 - 1.600 |
R-factor | 0.156 |
Rwork | 0.154 |
R-free | 0.20040 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1pnt |
RMSD bond length | 0.035 |
RMSD bond angle | 2.951 |
Data reduction software | XDS |
Data scaling software | Aimless (0.5.17) |
Phasing software | PHASER |
Refinement software | REFMAC |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 36.250 | 36.250 | 1.550 |
High resolution limit [Å] | 1.520 | 8.340 | 1.520 |
Rmerge | 0.080 | 0.053 | 0.388 |
Number of reflections | 24753 | ||
<I/σ(I)> | 9 | ||
Completeness [%] | 96.1 | 98.3 | 54.1 |
Redundancy | 4.2 | 4.1 | 2.5 |
CC(1/2) | 0.943 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | EVAPORATION | 6.5 | 293 | 20% PEG 3350, 0.2 M NaCl, Bis Tris, HEPES |