1L0F
X-ray Crystal Structure of AmpC N152H Mutant beta-Lactamase
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 5ID-B |
Synchrotron site | APS |
Beamline | 5ID-B |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2001-08-06 |
Detector | MARRESEARCH |
Wavelength(s) | 1.0 |
Spacegroup name | C 1 2 1 |
Unit cell lengths | 118.936, 76.260, 97.922 |
Unit cell angles | 90.00, 115.69, 90.00 |
Refinement procedure
Resolution | 20.000 - 1.660 |
Rwork | 0.178 |
R-free | 0.19800 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1fsy |
RMSD bond length | 0.014 |
RMSD bond angle | 1.750 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | CNS |
Refinement software | CNS |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.700 |
High resolution limit [Å] | 1.660 | 1.660 |
Rmerge | 0.060 | 0.217 |
Total number of observations | 369646 * | |
Number of reflections | 90254 | |
<I/σ(I)> | 32.8 | 5.3 |
Completeness [%] | 97.0 | 94.4 |
Redundancy | 4.1 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 8.7 | 296 | used to seeding, Usher, K.C., (1998) Biochemistry, 37, 16082. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | sodium potassium phosphate | 1.7 (M) | pH8.7 |
2 | 1 | drop | protein | 10 (mg/ml) |