8F28
Lysozyme Structures from Single-Entity Crystallization Method NanoAC
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-11-06 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 1.0000 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 78.592, 78.592, 36.815 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.690 - 1.200 |
R-factor | 0.144 |
Rwork | 0.142 |
R-free | 0.17030 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1iee |
RMSD bond length | 0.006 |
RMSD bond angle | 0.855 |
Data scaling software | HKL-2000 |
Phasing software | PHENIX (1.20) |
Refinement software | PHENIX (1.19.2_4158) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.220 |
High resolution limit [Å] | 1.200 | 3.260 | 1.200 |
Rmerge | 0.073 | 0.055 | 0.268 |
Rmeas | 0.079 | 0.060 | 0.346 |
Rpim | 0.028 | 0.022 | 0.215 |
Total number of observations | 246464 | ||
Number of reflections | 35301 | 1975 | 1298 |
<I/σ(I)> | 20.1 | ||
Completeness [%] | 96.4 | 97.3 | 71.2 |
Redundancy | 7 | 7.8 | 2 |
CC(1/2) | 0.993 | 0.852 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | LIQUID DIFFUSION | 4.8 | 295 | A new crystallization method named NanoAC was used. Protein solution and precipitant solution were connected through a single nanopipette to control (in time and space) nucleation and crystal growth |