1YTC
THERMODYNAMIC CYCLES AS PROBES OF STRUCTURE-FUNCTION RELATIONSHIPS IN UNFOLDED PROTEINS
Experimental procedure
Detector technology | IMAGE PLATE |
Collection date | 1992-03-24 |
Detector | RIGAKU |
Wavelength(s) | 1.5418 |
Spacegroup name | P 43 21 2 |
Unit cell lengths | 36.660, 36.660, 138.920 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 8.000 - 1.800 |
R-factor | 0.162 |
Rwork | 0.162 |
RMSD bond length | 0.020 |
RMSD bond angle | 0.036 * |
Data reduction software | R-AXIS ((MSC)) |
Phasing software | X-PLOR (3.1) |
Refinement software | PROLSQ |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 9999.000 * | |
High resolution limit [Å] | 1.800 | 1.800 * |
Rmerge | 0.060 | |
Total number of observations | 59573 * | |
Number of reflections | 9141 | |
Completeness [%] | 95.5 | 93.4 * |
Redundancy | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | unknown * | 7 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | 1 | protein | 20 (mg/ml) | |
2 | 1 | 2 | sodium phosphate | 0.1 (M) | |
3 | 1 | 2 | 0.3 (M) | ||
4 | 1 | 2 | dithiothreitol | 40 (mM) | |
5 | 1 | 2 | ammonium sulfate | 90 (%sat) |