7L2A
Molybdopterin cofactor biosynthesis protein E from Burkholderia multivorans ATCC 17616
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 21-ID-F |
Synchrotron site | APS |
Beamline | 21-ID-F |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2020-07-30 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.730, 72.660, 105.770 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 42.760 - 1.850 |
R-factor | 0.191 |
Rwork | 0.189 |
R-free | 0.22320 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 2QIE as per MoRDa |
RMSD bond length | 0.008 |
RMSD bond angle | 0.939 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | MoRDa |
Refinement software | PHENIX (1.19rc4) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 50.000 | 50.000 | 1.900 |
High resolution limit [Å] | 1.850 | 8.270 | 1.850 |
Rmerge | 0.042 | 0.032 | 0.407 |
Rmeas | 0.045 | 0.035 | 0.465 |
Number of reflections | 32130 | 422 | 2319 |
<I/σ(I)> | 23.12 | 49.55 | 2.88 |
Completeness [%] | 99.9 | 98.8 | 99.5 |
Redundancy | 6.821 | 5.78 | 4.241 |
CC(1/2) | 0.999 | 0.998 | 0.946 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 6.5 | 287 | Molecular Dimensions Morpheus screen, E3: 10% w/v PEG 4000, 20% v/v glycerol, 0.03 M of each diethyleneglycol, triethyleneglycol, tetraethyleneglycol, pentaethyleneglycol, 0.1 M MES/imidazole pH 6.5: BumuA.00098.a.B1.PS37859 at 41.7mg/ml + 0.5% beta-octyl-glucoside: cryo: direct: tray 317330e3, puck xxu3-3. |