1OEP
Structure of Trypanosoma brucei enolase reveals the inhibitory divalent metal site
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | ROTATING ANODE |
Source details | RIGAKU ULTRAX 18 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 2002-10-15 |
Detector | MARRESEARCH |
Spacegroup name | C 2 2 21 |
Unit cell lengths | 74.018, 110.536, 109.098 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 38.820 - 2.300 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.25100 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1one |
RMSD bond length | 0.007 |
RMSD bond angle | 23.100 * |
Data reduction software | AUTOMAR |
Data scaling software | AUTOMAR |
Phasing software | MOLREP |
Refinement software | CNS (1.0) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 38.800 * | 2.380 |
High resolution limit [Å] | 2.300 | 2.300 |
Rmerge | 0.065 | 0.468 |
Number of reflections | 20116 | |
<I/σ(I)> | 14.2 | 1.9 |
Completeness [%] | 97.2 * | 93.4 |
Redundancy | 4.7 | 4.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 6.5 | 18 * | Hannaert, V., (2003) Eur.J.Biochem., 270, 3205. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 6 (mg/ml) |