7FY9
Crystal Structure of human FABP4 binding site mutated to that of FABP5 in complex with 2-cyclopentyl-4-(4-fluorophenyl)-6-[1-(methoxymethyl)cyclopentyl]-3-methyl-5-(1H-tetrazol-5-yl)pyridine
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 100 |
Detector technology | PIXEL |
Collection date | 2012-09-22 |
Detector | PSI PILATUS 6M |
Wavelength(s) | 1.000040 |
Spacegroup name | P 2 21 21 |
Unit cell lengths | 31.672, 53.455, 72.409 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 43.006 - 1.740 |
R-factor | 0.2083 |
Rwork | 0.205 |
R-free | 0.27450 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | inhouse model |
RMSD bond length | 0.013 |
RMSD bond angle | 1.455 |
Data reduction software | XDS |
Data scaling software | XSCALE |
Phasing software | PHASER |
Refinement software | PHENIX (1.8.1_1168) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 43.010 | 43.006 | 1.790 |
High resolution limit [Å] | 1.740 | 7.780 | 1.740 |
Rmerge | 0.171 | 0.034 | 2.258 |
Rmeas | 0.164 | 0.037 | 2.451 |
Total number of observations | 80744 | ||
Number of reflections | 12988 | 187 | 924 |
<I/σ(I)> | 6.1 | 30.96 | 1.27 |
Completeness [%] | 98.2 | 98.4 | 96.8 |
Redundancy | 6.24 | 4.791 | 6.578 |
CC(1/2) | 0.997 | 0.998 | 0.446 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 293 | protein in 25mM Tris/HCl pH 7.5 100mM NaCl, see also PMID 27658368 |