2FD9
X-ray Crystal Structure of Chemically Synthesized Crambin-{alpha}carboxamide
Experimental procedure
Experimental method | SINGLE WAVELENGTH |
Source type | SYNCHROTRON |
Source details | APS BEAMLINE 5ID-B |
Synchrotron site | APS |
Beamline | 5ID-B |
Spacegroup name | H 3 2 |
Unit cell lengths | 67.581, 67.581, 39.487 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 20.000 - 1.600 |
R-factor | 0.2165 |
Rwork | 0.216 |
R-free | 0.23385 |
Structure solution method | MOLECULAR REPLACEMENT |
RMSD bond length | 0.015 |
RMSD bond angle | 1.547 |
Refinement software | REFMAC (5.1.9999) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 20.000 | 1.643 |
High resolution limit [Å] | 1.600 | 1.601 |
Number of reflections | 4354 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION, HANGING DROP | 7 | 277 | X-ray crystallography-quality crystals for crambin-carboxamide were formed by mixing 2 ul of protein (10 mg/ml in pH 7.5 100mM HEPES buffer containing 150 mM NaCl) and 2 ul of a 0.8 M succinic acid (used for X-ray diffraction), or by mixing 2 ul of the protein solution with 2 ul of 0.1 M HEPES buffer containing 15% v/v tacsimate and 2% w/v polyethylene glycol 3350, pH 7.0, VAPOR DIFFUSION, HANGING DROP, temperature 277K |