1QO1
Molecular Architecture of the Rotary Motor in ATP Synthase from Yeast Mitochondria
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID2 |
Synchrotron site | ESRF |
Beamline | ID2 |
Temperature [K] | 100 |
Detector technology | IMAGE PLATE |
Collection date | 1999-02-15 |
Detector | MARRESEARCH |
Spacegroup name | P 1 21 1 |
Unit cell lengths | 135.900, 175.300, 139.200 |
Unit cell angles | 90.00, 91.60, 90.00 |
Refinement procedure
Resolution | 15.000 * - 3.900 |
R-factor | 0.467 * |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1bmf |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | AMoRE |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 15.000 | 4.110 |
High resolution limit [Å] | 3.900 | 3.900 |
Rmerge | 0.100 | 0.372 * |
Number of reflections | 55593 | 8288 * |
<I/σ(I)> | 4 | 1.3 |
Completeness [%] | 93.3 | 95.5 |
Redundancy | 2.5 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Batch method * | 8 | 4 * | 0.1 M TRIS/CL PH8.0, 12% PEG 6000, 150 MM NACL, 1 MM AMP-PNP, 40 MICROM ADP, 1 MM DTT, 0.02% NAN3, MIXED 1:1 WITH PROTEIN SOLUTION UNDER PARAFFIN OIL IN MICROBATCH PLATE., pH 8.00 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 10 (mg/ml) | |
2 | 1 | 1 | Tris | 0.1 (M) | |
3 | 1 | 1 | PEG6000 | 12 (%) | |
4 | 1 | 1 | 150 (mM) | ||
5 | 1 | 1 | AMP-PNP | 1 (mM) | |
6 | 1 | 1 | ADP | 0.040 (mM) | |
7 | 1 | 1 | dithiothreitol | 1 (mM) | |
8 | 1 | 1 | sodium azide | 0.02 (%) |