3CMT
Mechanism of homologous recombination from the RecA-ssDNA/dsDNA structures
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | APS BEAMLINE 24-ID-C |
| Synchrotron site | APS |
| Beamline | 24-ID-C |
| Collection date | 2007-07-01 |
| Spacegroup name | P 21 21 2 |
| Unit cell lengths | 159.000, 300.500, 80.100 |
| Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
| Resolution | 40.000 - 3.150 |
| R-factor | 0.218 |
| Rwork | 0.217 |
| R-free | 0.24300 |
| Structure solution method | MOLECULAR REPLACEMENT |
| RMSD bond length | 0.008 |
| RMSD bond angle | 1.170 |
| Refinement software | REFMAC (5.3.0036) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 40.000 |
| High resolution limit [Å] | 3.150 |
| Number of reflections | 59390 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 8 | the RecA5 fusion protein was incubated with a 1.5-fold molar excess of the primary d(T5C3AC2T4) oligonucleotide in protein buffer supplemented with 2 mM ADP, 10 mM MgCl2 and 8 mM AlF4, pH 6.0, for 30 min, followed by the addition of 2-fold molar excess of the complementary d(G2TG3) oligonucleotide. The crystals grew from 50 mM Tris-Cl, 9% (w/v) PVP K15, 32% (v/v) MPD, 100 mM magnesium acetate, 10 mM DTT, pH 8.0. |
Crystallization Reagents
| ID | crystal ID | solution ID | reagent name | concentration | details |
| 1 | 1 | 1 | ADP | ||
| 10 | 1 | 2 | PVP K15 | ||
| 11 | 1 | 2 | MPD | ||
| 12 | 1 | 2 | magnesium acetate | ||
| 13 | 1 | 2 | 10 mM DTT | ||
| 2 | 1 | 1 | MgCl2 | ||
| 3 | 1 | 1 | AlF4 | ||
| 4 | 1 | 1 | Tris-Cl | ||
| 5 | 1 | 1 | PVP K15 | ||
| 6 | 1 | 1 | MPD | ||
| 7 | 1 | 1 | magnesium acetate | ||
| 8 | 1 | 1 | 10 mM DTT | ||
| 9 | 1 | 2 | Tris-Cl |
