2A6A
Crystal structure of Glycoprotein endopeptidase (tm0874) from THERMOTOGA MARITIMA at 2.50 A resolution
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | SSRL BEAMLINE BL11-1 |
Synchrotron site | SSRL |
Beamline | BL11-1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-04-03 |
Detector | ADSC QUANTUM 315 |
Wavelength(s) | 0.979413, 0.918370 |
Spacegroup name | C 2 2 2 |
Unit cell lengths | 93.272, 217.112, 51.953 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 29.240 - 2.500 |
Rwork | 0.191 |
R-free | 0.23500 |
Structure solution method | MAD |
RMSD bond length | 0.018 |
RMSD bond angle | 1.688 |
Data reduction software | XDS |
Data scaling software | SCALA |
Phasing software | SHELXD |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 29.240 | 29.240 | 2.640 |
High resolution limit [Å] | 2.500 | 7.910 | 2.500 |
Rmerge | 0.051 | 0.018 | 0.469 |
Number of reflections | 18685 | ||
<I/σ(I)> | 11.7 | 34.4 | 1.6 |
Completeness [%] | 99.6 | ||
Redundancy | 3.6 | 3 | 3.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION,SITTING DROP,NANODROP | 4 | 273 | 10.0% MPD, 0.1M Citrate pH 4.0, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 273K |