1VRM
Crystal structure of the apbe protein (tm1553) from thermotoga maritima msb8 at 1.58 A resolution
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | ALS BEAMLINE 8.2.1 |
Synchrotron site | ALS |
Beamline | 8.2.1 |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 2005-01-22 |
Detector | ADSC QUANTUM 210 |
Wavelength(s) | 0.97950,1.00003 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 57.742, 76.946, 86.587 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 20.610 - 1.580 |
Rwork | 0.157 |
R-free | 0.19100 |
Structure solution method | MAD |
RMSD bond length | 0.017 |
RMSD bond angle | 1.564 |
Data reduction software | MOSFLM |
Data scaling software | SCALA |
Phasing software | SOLVE |
Refinement software | REFMAC (5.2.0005) |
Data quality characteristics
Overall | Inner shell | Outer shell | |
Low resolution limit [Å] | 20.610 | 20.610 | 1.620 |
High resolution limit [Å] | 1.500 | 7.070 | 1.580 |
Rmerge | 0.096 | 0.050 | 0.703 |
Number of reflections | 51395 | ||
<I/σ(I)> | 5 | 11.5 | 0.9 |
Completeness [%] | 96.2 | ||
Redundancy | 3.2 | 3.1 | 1.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | VAPOR DIFFUSION,SITTING DROP,NANODROP | 5 | 277 | 10.0% MPD, 0.1M Citrate pH 5.0, VAPOR DIFFUSION,SITTING DROP,NANODROP, temperature 277K |