1OHQ
Crystal structure of HEL4, a soluble human VH antibody domain resistant to aggregation
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF |
Synchrotron site | ESRF |
Temperature [K] | 100 |
Collection date | 2002-09-15 |
Spacegroup name | I 41 2 2 |
Unit cell lengths | 76.121, 76.121, 187.069 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 70.000 - 2.000 |
R-factor | 0.182 |
Rwork | 0.182 |
R-free | 0.25600 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fgv |
RMSD bond length | 0.007 * |
RMSD bond angle | 1.400 * |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Refinement software | REFMAC |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 70.000 | 2.110 |
High resolution limit [Å] | 2.000 | 2.000 |
Rmerge | 0.143 * | 0.667 * |
Number of reflections | 19067 | |
<I/σ(I)> | 4.3 | 2.2 |
Completeness [%] | 99.7 * | 96 * |
Redundancy | 7.0 * | 6.0 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.2 * | pH 6.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 22.3 (mg/ml) | |
2 | 1 | reservoir | HEPES | 0.1 (M) | pH7.2 |
3 | 1 | reservoir | 1.6 (M) | ||
4 | 1 | reservoir | glycerol | 6 (%(v/v)) |