2VOR
Crystal Structures of Mycobacterium tuberculosis Folylpolyglutamate Synthase Complexed with ADP and AMPPCP
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL9-1 |
| Synchrotron site | SSRL |
| Beamline | BL9-1 |
| Temperature [K] | 100 |
| Detector technology | CCD |
| Collection date | 2006-02-26 |
| Detector | ADSC CCD |
| Spacegroup name | P 21 3 |
| Unit cell lengths | 112.396, 112.396, 112.396 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 79.560 - 2.300 |
| R-factor | 0.178 |
| Rwork | 0.176 |
| R-free | 0.22300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | MTBFPGS ADP STRUCTURE USED AS A MODEL FOR MOLECULAR REPLACEMENT |
| RMSD bond length | 0.023 |
| RMSD bond angle | 2.057 |
| Data reduction software | MOSFLM |
| Data scaling software | SCALA |
| Phasing software | PHASER |
| Refinement software | REFMAC (5.4.0067) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 56.200 | 2.420 |
| High resolution limit [Å] | 2.300 | 2.300 |
| Rmerge | 0.100 | 0.660 |
| Number of reflections | 21320 | |
| <I/σ(I)> | 14.1 | 2.9 |
| Completeness [%] | 100.0 | 100 |
| Redundancy | 7.1 | 7.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 5.5 | MTBFPGS PRE-INCUBATED WITH 1.5 MM ADP AND 2 MM MGCL2 WERE GROWN BY THE BATCH METHOD UNDER PARAFFIN OIL IN 2 PLUS 2 UL DROPS OF PROTEIN AND 14%(W/V) PEG 8000, 30%(V/V) MPD, 10 MM COCL2, 50 MM SODIUM ACETATE PH 5.5 |
