3MAC
crystal structure of GP41-derived protein complexed with fab 8062
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 22-ID |
Synchrotron site | APS |
Beamline | 22-ID |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2009-01-01 |
Detector | MARCCD300 |
Wavelength(s) | 1.0 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 83.668, 41.741, 98.602 |
Unit cell angles | 90.00, 94.85, 90.00 |
Refinement procedure
Resolution | 29.500 - 2.500 |
R-factor | 0.20163 |
Rwork | 0.200 |
R-free | 0.26441 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2cmr |
RMSD bond length | 0.010 |
RMSD bond angle | 1.190 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | PHASER |
Refinement software | REFMAC (5.5.0104) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 29.500 | 2.590 |
High resolution limit [Å] | 2.500 | 2.500 |
Number of reflections | 23655 | |
<I/σ(I)> | 13.79 | 2 |
Completeness [%] | 99.1 | 96.7 |
Redundancy | 3.1 | 3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8 | 293 | 14% Polyethylene glycol 10K, 0.1M ammonium sulfate, 5% ethylene glycol, pH 8.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K |