5AZA
Crystal structure of MBP-sAglB fusion protein with a 20-residue spacer in the connector helix
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL32XU |
| Synchrotron site | SPring-8 |
| Beamline | BL32XU |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2012-05-27 |
| Detector | RAYONIX MX-225 |
| Wavelength(s) | 1.0 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 66.468, 100.467, 140.920 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 50.000 - 2.080 |
| R-factor | 0.19845 |
| Rwork | 0.196 |
| R-free | 0.24821 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1anf 2zai |
| RMSD bond length | 0.017 |
| RMSD bond angle | 1.854 |
| Data reduction software | HKL-2000 |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 50.000 |
| High resolution limit [Å] | 2.080 |
| Number of reflections | 57642 |
| <I/σ(I)> | 18.7 |
| Completeness [%] | 100.0 |
| Redundancy | 12 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 5.5 | 293 | 17% PEG 10000, 0.1M Ammounium phosphate, 0.1M Bis-Tris pH5.5, 1.0M Lithium chloride |
