1OQO
Complex between G0 version of an Fc bound to a minimized version of Protein A called Mini-Z
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL9-1 |
Synchrotron site | SSRL |
Beamline | BL9-1 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1998-04-27 |
Detector | MARRESEARCH |
Wavelength(s) | 1.08 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 85.782, 126.413, 54.743 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.000 - 2.300 |
R-factor | 0.216 |
Rwork | 0.216 |
R-free | 0.28600 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1l6x |
RMSD bond length | 0.010 |
RMSD bond angle | 1.500 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | X-PLOR (98.1) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 99.000 | 2.370 |
High resolution limit [Å] | 2.300 | 2.290 |
Number of reflections | 27051 | |
Completeness [%] | 99.7 | 95.4 |
Redundancy | 4 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 5.5 | 323 | 20% PEG 550 MME, 0.1M NaOAc, 0.25M NaCl, pH 5.5, VAPOR DIFFUSION, SITTING DROP, temperature 323K |