6LFP
Cry3Aa protein for enzyme entrapment
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | NSRRC BEAMLINE TPS 05A |
| Synchrotron site | NSRRC |
| Beamline | TPS 05A |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2019-04-10 |
| Detector | RAYONIX MX300-HS |
| Wavelength(s) | 1.0 |
| Spacegroup name | C 2 2 21 |
| Unit cell lengths | 116.350, 132.610, 102.890 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 38.340 - 3.310 |
| R-factor | 0.1594 |
| Rwork | 0.157 |
| R-free | 0.20890 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1dlc |
| RMSD bond length | 0.013 |
| RMSD bond angle | 1.714 |
| Data reduction software | MOSFLM |
| Data scaling software | Aimless (0.5.17) |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.8.0135) |
Data quality characteristics
| Overall | Inner shell | Outer shell | |
| Low resolution limit [Å] | 87.460 | 38.340 | 3.580 |
| High resolution limit [Å] | 3.310 | 8.760 | 3.310 |
| Rmerge | 0.141 | 0.077 | 0.285 |
| Rmeas | 0.163 | 0.090 | 0.330 |
| Rpim | 0.080 | 0.045 | 0.162 |
| Total number of observations | 2364 | 9572 | |
| Number of reflections | 12048 | 690 | 2457 |
| <I/σ(I)> | 7.7 | 11.9 | 4.6 |
| Completeness [%] | 98.9 | 95.2 | 99.8 |
| Redundancy | 3.9 | 3.4 | 3.9 |
| CC(1/2) | 0.979 | 0.986 | 0.918 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 4.8 | 291 | 0.1M NaOAc pH 4.8, 2.2M NaCl |
