4LIL
Crystal structure of the catalytic subunit of human primase bound to UTP and Mn
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-11-16 |
Detector | MARMOSAIC 225 mm CCD |
Wavelength(s) | 0.9787 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 79.346, 79.346, 148.200 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 44.731 - 2.600 |
R-factor | 0.2153 |
Rwork | 0.214 |
R-free | 0.24840 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.011 |
RMSD bond angle | 1.327 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | PHASER |
Refinement software | PHENIX ((phenix.refine: 1.8.2_1309)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Number of reflections | 15266 | |
<I/σ(I)> | 37.6 | 6.1 |
Completeness [%] | 100.0 | 100 |
Redundancy | 14.2 | 14.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 294 | 0.2M K/Na Tartrate and 20% PEG 3350, pH 7.0, VAPOR DIFFUSION, SITTING DROP, temperature 294K |