4PF0
Structure of the E502A variant of sacteLam55A from Streptomyces sp. SirexAA-E in complex with laminarihexaose
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 21-ID-G |
| Synchrotron site | APS |
| Beamline | 21-ID-G |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-08-08 |
| Detector | MARMOSAIC 300 mm CCD |
| Wavelength(s) | 0.97857 |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 54.098, 100.960, 104.176 |
| Unit cell angles | 90.00, 91.09, 90.00 |
Refinement procedure
| Resolution | 30.300 - 1.750 |
| R-factor | 0.152 |
| Rwork | 0.151 |
| R-free | 0.18200 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 4pew |
| RMSD bond length | 0.007 |
| RMSD bond angle | 1.134 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | PHASER |
| Refinement software | PHENIX ((PHENIX.REFINE: 1.8.4_1496)) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 50.000 | 1.670 |
| High resolution limit [Å] | 1.640 | 1.640 |
| Rmerge | 0.096 | 0.448 |
| Number of reflections | 136258 | |
| <I/σ(I)> | 6.6 | |
| Completeness [%] | 99.5 | 96.9 |
| Redundancy | 4 | 3.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 6 | 298 | Protein Solution (20 mg/ml protein, 0.05 M NaCl, and 0.010 M MOPS pH 7) mixed in a 1:1 ratio with the Well Solution (20% PEG 3350, 200mM NaC2H302, and 100mM BTP pH 6.0). Cryoprotected with 20% PEG 3350, 200mM NaC2H302, 25mM laminaritetraose, 100mM BTP pH 6.0 and 15% ethylene glycol |
