5F1X
Crystal structure of human GRP78 (70kDa heat shock protein 5 / BIP) ATPase domain in complex with ATP
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 23-ID-B |
Synchrotron site | APS |
Beamline | 23-ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2015-07-10 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 1.0332 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 55.965, 74.823, 90.222 |
Unit cell angles | 90.00, 98.85, 90.00 |
Refinement procedure
Resolution | 44.470 - 1.900 |
R-factor | 0.1832 |
Rwork | 0.181 |
R-free | 0.22790 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5exw |
RMSD bond length | 0.011 |
RMSD bond angle | 1.273 |
Data reduction software | XDS |
Data scaling software | SCALA (3.3.21) |
Phasing software | MOLREP |
Refinement software | REFMAC (5.7.0032) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 44.470 | 44.472 | 2.000 |
High resolution limit [Å] | 1.900 | 6.010 | 1.900 |
Rmerge | 0.053 | 0.654 | |
Rmeas | 0.131 | ||
Rpim | 0.067 | 0.033 | 0.390 |
Total number of observations | 219077 | 6882 | 32144 |
Number of reflections | 58009 | ||
<I/σ(I)> | 8.3 | 19 | 2.2 |
Completeness [%] | 99.9 | 99.4 | 100 |
Redundancy | 3.8 | 3.6 | 3.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.5 | 289 | 24-26% PEG3350, 0.1 M Tris-HCl, 0.2 M sodium chloride |