2VEO
X-ray structure of Candida antarctica lipase A in its closed state.
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | ESRF BEAMLINE ID29 |
Synchrotron site | ESRF |
Beamline | ID29 |
Temperature [K] | 110 |
Detector technology | CCD |
Collection date | 2006-05-15 |
Detector | ADSC CCD |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 91.539, 91.539, 299.842 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 30.000 - 2.200 |
R-factor | 0.192 |
Rwork | 0.190 |
R-free | 0.22100 |
Structure solution method | SIRAS |
Starting model (for MR) | NONE |
RMSD bond length | 0.006 |
RMSD bond angle | 0.937 |
Data scaling software | SCALA |
Phasing software | SHELXD |
Refinement software | REFMAC (5.2.0019) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 30.000 | 2.320 |
High resolution limit [Å] | 2.200 | 2.200 |
Rmerge | 0.140 | 0.620 |
Number of reflections | 63098 | |
<I/σ(I)> | 10.2 | 2 |
Completeness [%] | 96.0 | 85.3 |
Redundancy | 4 | 2.5 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 6.4 | 2 MICROLITER 10 MILLIGRAM/MILLILITER PROTEIN IN 0.002M TRIS-HCL, PH 8.0 MIXED WITH 1 MICROLITER 0.2M AMMONIUM SULFATE, 0.1M BIS-TRIS, PH 5.5, AND 25% (W/V) PEG 3350. |