1OR0
Crystal Structures of Glutaryl 7-Aminocephalosporanic Acid Acylase: Insight into Autoproteolytic Activation
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X9B |
Synchrotron site | NSLS |
Beamline | X9B |
Wavelength(s) | 0.9810, 0.9800, 0.9680 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 229.667, 69.907, 113.726 |
Unit cell angles | 90.00, 97.63, 90.00 |
Refinement procedure
Resolution | 20.000 * - 2.000 |
R-factor | 0.189 |
Rwork | 0.171 |
R-free | 0.20600 * |
Structure solution method | MAD |
RMSD bond length | 0.005 |
RMSD bond angle | 23.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS (1.1) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 20.000 * |
High resolution limit [Å] | 2.000 |
Number of reflections | 110770 * |
Completeness [%] | 91.8 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7.5 | 20 * | 0.6M ammonium sulfate, 0.1M HEPES, and 0.1M NaCl, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 293.0K |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | ammonium sulfate | 1.6 (M) | |
2 | 1 | reservoir | HEPES | 0.1 (M) | pH7.5 |
3 | 1 | reservoir | 0.1 (M) |