5HD2
The crystal structure of SeMet-Cry51Aa2-L11M
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-D |
Synchrotron site | APS |
Beamline | 21-ID-D |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2007-12-12 |
Detector | MAR scanner 300 mm plate |
Wavelength(s) | 1.000 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 55.567, 55.567, 208.962 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 53.700 - 2.276 |
R-factor | 0.23813 |
Rwork | 0.235 |
R-free | 0.29458 |
Structure solution method | MAD |
RMSD bond length | 0.019 |
RMSD bond angle | 1.798 |
Data reduction software | HKL-2000 |
Data scaling software | HKL-2000 |
Phasing software | SOLVE (2.08) |
Refinement software | REFMAC (5.5.0102) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 53.700 | 2.350 |
High resolution limit [Å] | 2.270 | 2.270 |
Rmerge | 0.094 | 0.381 |
Number of reflections | 15236 | |
<I/σ(I)> | 17.4 | 1.75 |
Completeness [%] | 95.9 | 96.4 |
Redundancy | 4.7 | 4.9 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7.5 | 293 | Starting protein solution was 5.5 mg/ml protein in 25 mM sodium carbonate buffer-pH 10.5. The reservoir solution was 500 ul of 2.0 M sodium chloride and 50 mM HEPES-pH 7.5 buffer. Bipyramidal crystals resulted from 2 ul drops, using 0.7 ul protein solution and 1.3 ul well solution. |