1PFF
Crystal Structure of Homocysteine alpha-, gamma-lyase at 1.8 Angstroms
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | SSRL BEAMLINE BL7-1 |
| Synchrotron site | SSRL |
| Beamline | BL7-1 |
| Spacegroup name | C 1 2 1 |
| Unit cell lengths | 166.634, 48.476, 75.606 |
| Unit cell angles | 90.00, 110.33, 90.00 |
Refinement procedure
| Resolution | 32.500 - 2.500 |
| R-factor | 0.17975 |
| Rwork | 0.179 |
| R-free | 0.20837 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1e5f |
| RMSD bond length | 0.009 |
| RMSD bond angle | 1.139 |
| Data reduction software | MOSFLM |
| Data scaling software | CCP4 ((SCALA)) |
| Phasing software | AMoRE |
| Refinement software | REFMAC (5.1.27) |
Data quality characteristics
| Overall | |
| Low resolution limit [Å] | 32.500 |
| High resolution limit [Å] | 2.500 |
| Number of reflections | 19864 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 100 mM HEPES/NaOH (ph 7.5), 100 mM MgCl2, 15% w/v MPEG 2000, VAPOR DIFFUSION, HANGING DROP |
