1AY1
ANTI TAQ FAB TP7
Experimental procedure
| Source type | ROTATING ANODE |
| Source details | MACSCIENCE |
| Temperature [K] | 293 |
| Detector technology | AREA DETECTOR |
| Collection date | 1995-10 |
| Detector | SIEMENS |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 36.500, 72.700, 82.200 |
| Unit cell angles | 90.00, 98.40, 90.00 |
Refinement procedure
| Resolution | 7.000 - 2.200 |
| R-factor | 0.196 |
| Rwork | 0.196 |
| R-free | 0.28800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1hil |
| RMSD bond length | 0.008 |
| RMSD bond angle | 18.600 * |
| Data reduction software | XDS |
| Data scaling software | XDS |
| Phasing software | AMoRE |
| Refinement software | X-PLOR (3.1) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 2.300 |
| High resolution limit [Å] | 2.200 | 2.200 |
| Rmerge | 0.078 | 0.112 |
| Number of reflections | 50786 | |
| <I/σ(I)> | 12.8 | 4.8 |
| Completeness [%] | 83.0 | 68.2 |
| Redundancy | 3 | 2.1 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | Vapor diffusion, hanging drop * | 9 | 20 * | PROTEIN WAS CRYSTALLIZED FROM 16% PEG3350, 0.4% BETA OCTYL GLUCOSIDE, 100MM TRIS, PH 9.0 |
Crystallization Reagents in Literatures
| ID | crystal ID | solution | reagent name | concentration (unit) | details |
| 1 | 1 | drop | protein | 2.5 (mg/ml) | |
| 2 | 1 | drop | beta-octylglucoside | 0.2 (%) | |
| 3 | 1 | drop | Tris-HCl | 60 (mM) | |
| 4 | 1 | drop | PEG3350 | 8 (%) | |
| 5 | 1 | reservoir | PEG3350 | 16 (%) | |
| 6 | 1 | reservoir | Tris-HCl | 100 (mM) |
