5B27
The 1.02A structure of human FABP3 M20S mutant complexed with palmitic acid
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SPRING-8 BEAMLINE BL38B1 |
| Synchrotron site | SPring-8 |
| Beamline | BL38B1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2013-01-29 |
| Detector | ADSC QUANTUM 315 |
| Wavelength(s) | 0.9000 |
| Spacegroup name | P 21 21 21 |
| Unit cell lengths | 54.604, 70.057, 33.921 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 43.070 - 1.020 |
| R-factor | 0.11402 |
| Rwork | 0.113 |
| R-free | 0.12914 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 2hmb |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.499 |
| Data reduction software | HKL-2000 |
| Data scaling software | HKL-2000 |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 43.070 | 1.040 |
| High resolution limit [Å] | 1.020 | 1.020 |
| Rmerge | 0.090 | 0.370 |
| Number of reflections | 66771 | |
| <I/σ(I)> | 7 | 3.7 |
| Completeness [%] | 99.5 | 99.9 |
| Redundancy | 99.5 | 9.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, SITTING DROP | 8 | 293 | 0.1M Tris-HCl (pH8.0), 45% (v/v) PEG 400 |
