7U0S
Crystal Structure of FK506-binding protein 1A from Aspergillus fumigatus Bound to Ascomycin
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 | 2021-09-16 |
Detector | RAYONIX MX-300 |
Wavelength(s) | 0.97872 |
Spacegroup name | P 21 21 2 |
Unit cell lengths | 89.810, 91.470, 35.530 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 40.750 - 1.700 |
R-factor | 0.1697 |
Rwork | 0.168 |
R-free | 0.19210 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 5hwc |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.20-4438) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 40.750 | 40.750 | 1.740 |
High resolution limit [Å] | 1.700 | 7.600 | 1.700 |
Rmerge | 0.066 | 0.044 | 0.530 |
Rmeas | 0.075 | 0.051 | 0.593 |
Total number of observations | 159338 | ||
Number of reflections | 32881 | 424 | 2347 |
<I/σ(I)> | 13.78 | 29.32 | 2.9 |
Completeness [%] | 99.5 | 96.1 | 99.2 |
Redundancy | 4.846 | 4.127 | 4.915 |
CC(1/2) | 0.998 | 0.996 | 0.882 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 4.5 | 287 | [Barcode: 321029a1] [pin_id: kzq0-6] [collection: aps21idf 9/16/2021] [crystallization conditions: JCSG+ A1 - 0.2M lithium sulfate, pH 4.5, 50% (v/v) PEG 400] [cryo: direct] |