1PT9
Crystal Structure Analysis of the DIII Component of Transhydrogenase with a Thio-Nicotinamide Nucleotide Analogue
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID14-1 |
Synchrotron site | ESRF |
Beamline | ID14-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Spacegroup name | P 41 2 2 |
Unit cell lengths | 57.400, 57.400, 251.130 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.820 * - 2.420 |
Rwork | 0.219 |
R-free | 0.27800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1djl |
RMSD bond length | 0.007 |
RMSD bond angle | 1.247 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 36.820 | 2.550 |
High resolution limit [Å] | 2.420 | 2.420 |
Rmerge | 0.077 * | 0.319 * |
Total number of observations | 100817 * | |
Number of reflections | 16825 * | 2312 * |
<I/σ(I)> | 6.8 | 2.2 |
Completeness [%] | 98.5 | 96.2 |
Redundancy | 6.0 * | 4.9 * |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7 | unpublished data, White, S.A., (2000) Structure Fold.Des., 8, 1. * |