4Y7D
Alpha/beta hydrolase fold protein from Nakamurella multipartita
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 19-BM |
Synchrotron site | APS |
Beamline | 19-BM |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2012-07-16 |
Detector | ADSC QUANTUM 315r |
Wavelength(s) | 0.9792 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 67.404, 75.394, 126.536 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 36.100 - 1.680 |
R-factor | 0.1549 |
Rwork | 0.153 |
R-free | 0.18700 |
Structure solution method | SAD |
RMSD bond length | 0.014 |
RMSD bond angle | 1.619 |
Data reduction software | HKL-3000 |
Data scaling software | HKL-3000 |
Phasing software | HKL-3000 |
Refinement software | REFMAC (5.8.0073) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 36.100 | 50.000 | 1.710 |
High resolution limit [Å] | 1.680 | 4.560 | 1.680 |
Rmerge | 0.083 | 0.059 | 0.636 |
Rmeas | 0.091 | 0.065 | 0.748 |
Rpim | 0.037 | 0.026 | 0.386 |
Total number of observations | 417774 | ||
Number of reflections | 73782 | ||
<I/σ(I)> | 14.3 | 1.9 | |
Completeness [%] | 99.5 | 98.8 | 95.4 |
Redundancy | 5.7 | 5.9 | 3.4 |
CC(1/2) | 0.996 | 0.786 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, SITTING DROP | 7 | 289 | 0.1 M Bis-Tris Porpane -NaOH buffer, 1.2 M DL-malic acid |