3OTH
Crystal Structure of CalG1, Calicheamicin Glycostyltransferase, TDP and calicheamicin alpha3I bound form
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 | CCD |
Collection date | 2010-07-09 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9794 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 45.809, 100.100, 169.881 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.121 - 2.301 |
R-factor | 0.1968 |
Rwork | 0.194 |
R-free | 0.24660 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.005 |
RMSD bond angle | 0.955 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHENIX (Phaser) |
Refinement software | PHENIX (1.6.1_357) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.340 |
High resolution limit [Å] | 2.300 | 6.240 | 2.300 |
Rmerge | 0.126 | 0.089 | 0.313 |
Number of reflections | 34067 | ||
<I/σ(I)> | 6 | ||
Completeness [%] | 95.9 | 99.9 | 74.7 |
Redundancy | 6.6 | 6.6 | 4.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 298 | Protein Solution (20mg/ml CalG1 protein, 20mM Tris pH 8, 25mM TDP) mixed in a 1:1 ratio with the well solution (16% MEPEG5K, 160mM CaCl2, 100mM MES/Acetate pH 5.5) Cryoprotected with 20% Glycerol, 24% MEPEG5K, 160mM CaCl2, 100mM MES/Acetate pH 5.5, vapor diffusion, hanging drop, temperature 298K, VAPOR DIFFUSION, HANGING DROP |