4ACR
Crystal structure of N-glycosylated, C-terminally truncated human glypican-1
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | MAX II BEAMLINE I911-2 |
Synchrotron site | MAX II |
Beamline | I911-2 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2011-02-14 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 47.170, 168.630, 147.760 |
Unit cell angles | 90.00, 94.59, 90.00 |
Refinement procedure
Resolution | 29.714 - 2.550 |
R-factor | 0.253 |
Rwork | 0.251 |
R-free | 0.29200 |
Structure solution method | MAD |
Starting model (for MR) | NONE |
RMSD bond length | 0.003 |
RMSD bond angle | 0.717 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | Auto-Rickshaw |
Refinement software | PHENIX ((PHENIX.REFINE)) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.640 |
High resolution limit [Å] | 2.490 | 2.490 |
Rmerge | 0.080 | 0.680 |
Number of reflections | 79825 | |
<I/σ(I)> | 11.6 | 2.4 |
Completeness [%] | 98.9 | 94.9 |
Redundancy | 4.1 | 3.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 8 | 12-14% PEG 6000, 0.1 M TRIS-HCL, 0.2 M CACL2, PH 8.0 |