4BGV
1.8 A resolution structure of the malate dehydrogenase from Picrophilus torridus in its apo form
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE BM30A |
Synchrotron site | ESRF |
Beamline | BM30A |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2010-11-27 |
Detector | ADSC QUANTUM 315r |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 81.167, 81.167, 395.990 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 46.473 - 1.811 |
R-factor | 0.1483 |
Rwork | 0.146 |
R-free | 0.18480 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | ONE POLY-ALA MONOMER OF OUR PREVIOUS SIRAS PTMALDH MODEL |
RMSD bond length | 0.008 |
RMSD bond angle | 1.096 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | PHASER (2.1.4) |
Refinement software | PHENIX |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 46.470 | 1.910 |
High resolution limit [Å] | 1.810 | 1.810 |
Rmerge | 0.120 | 0.670 |
Number of reflections | 121716 | |
<I/σ(I)> | 6.3 | 1.3 |
Completeness [%] | 99.8 | 98.5 |
Redundancy | 11.5 | 10.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 3.5 | 293 | 9-14 % PEG 4000, 0.1 M CITRIC ACID PH 3.5, 293 K, 12-15 DAYS |