4BFH
Crystal structure of alpha-amylase inhibitor wrightide R1 (wR1) peptide from Wrightia religiosa
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | SLS BEAMLINE X10SA |
Synchrotron site | SLS |
Beamline | X10SA |
Temperature [K] | 93 |
Detector technology | CCD |
Collection date | 2013-02-24 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 16.194, 29.133, 47.701 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 24.860 - 1.250 |
R-factor | 0.15787 |
Rwork | 0.158 |
R-free | 0.15927 |
Structure solution method | MOLECULAR REPLACEMENT |
Starting model (for MR) | 1clv |
RMSD bond length | 0.006 |
RMSD bond angle | 0.971 |
Refinement software | REFMAC (5.5.0110) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 25.000 | 1.320 |
High resolution limit [Å] | 1.250 | 1.250 |
Rmerge | 0.030 | 0.070 |
Number of reflections | 6362 | |
<I/σ(I)> | 23.2 | 11.9 |
Completeness [%] | 95.4 | 90.3 |
Redundancy | 3.3 | 3.3 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | 2 | pH 2 |