2EX1
Crystal structure of mutifunctional sialyltransferase from Pasteurella multocida with CMP bound
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-2 |
| Synchrotron site | SSRL |
| Beamline | BL9-2 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2005-07-22 |
| Detector | MARRESEARCH |
| Wavelength(s) | 0.97931 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 61.255, 64.571, 64.840 |
| Unit cell angles | 90.00, 98.62, 90.00 |
Refinement procedure
| Resolution | 38.390 - 2.000 |
| R-factor | 0.192 |
| Rwork | 0.192 |
| R-free | 0.22200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1ex0 |
| RMSD bond length | 0.006 |
| RMSD bond angle | 1.200 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | CNS (1.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 64.150 | 2.050 |
| High resolution limit [Å] | 2.000 | 2.000 |
| Rmerge | 0.045 | 0.170 |
| Number of reflections | 33403 | |
| <I/σ(I)> | 17.8 | 5.4 |
| Completeness [%] | 98.3 | 97.7 |
| Redundancy | 3.8 | 3.8 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 298 | 0.216 mM protein, 26% PEG3350, 0.1M NaCl, 0.4% Triton-X-100, 0.1M HEPES, 2 mM CMP-sialic acid, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K |
