3RSC
Crystal Structure of CalG2, Calicheamicin Glycosyltransferase, TDP and calicheamicin T0 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 | 2011-02-14 |
Detector | MARMOSAIC 300 mm CCD |
Wavelength(s) | 0.9794 |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 88.289, 48.592, 108.393 |
Unit cell angles | 90.00, 101.71, 90.00 |
Refinement procedure
Resolution | 37.465 - 2.190 |
R-factor | 0.1985 |
Rwork | 0.197 |
R-free | 0.23950 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.007 |
RMSD bond angle | 1.149 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASER |
Refinement software | PHENIX (1.6.4_486) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 2.240 |
High resolution limit [Å] | 2.190 | 5.970 | 2.200 |
Rmerge | 0.109 | 0.050 | 0.604 |
Number of reflections | 46619 | ||
<I/σ(I)> | 7.7 | ||
Completeness [%] | 99.8 | 99.9 | 97.6 |
Redundancy | 5.2 | 4.9 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 298 | Protein Solution (20 mg/ml CalG2 protein, 0.05M NaCl, 0.015M Tris pH 8) mixed in a 1:1 ratio with the well solution (0.5% MEPEG5K, 800mM Na K-tartrate, 100mM Tris pH 8.5) Cryoprotected with 20% Ethylene Glycol, 0.5% MEPEG5K, 800mM Na K-tartrate, 100mM Tris pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |