1T2J
Crystal structure of a Human VH domain
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE X31 |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | X31 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2003-07-05 |
Detector | MARRESEARCH |
Wavelength(s) | 0.802 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 71.336, 37.965, 37.187 |
Unit cell angles | 90.00, 109.67, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.500 |
R-factor | 0.15979 |
Rwork | 0.158 |
R-free | 0.19652 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1HOU |
RMSD bond length | 0.018 |
RMSD bond angle | 1.735 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | AMoRE |
Refinement software | REFMAC (5.1.24) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 34.922 | 1.530 |
High resolution limit [Å] | 1.500 | 1.500 |
Rmerge | 0.047 | 0.214 |
Number of reflections | 15017 | |
<I/σ(I)> | 27.69 | 7.26 |
Completeness [%] | 90.7 | 92.9 |
Redundancy | 4.29 | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 6.5 | 277 | Crystals grew from 3 microlitre hangingdrop formed by mixing 1.5 microlitre of protein:subtilisin mixture (250:1 M ratio) at protein conc. 13.5 mg/ml with 1.5 microlitre of reservoir solution 100mM MES, pH6.5, 10mM ZnSO4, 25% v/v PEG550MME, 4mM DTT and 0.04% v/v NaN3, VAPOR DIFFUSION, HANGING DROP, temperature 277K |