2MSP
MAJOR SPERM PROTEIN, BETA ISOFORM, ENGINEERED C59S/T90C MUTANT, PUTATIVE SUBFILAMENT STRUCTURE, PH 8.5
Experimental procedure
Source type | SYNCHROTRON |
Source details | SRS BEAMLINE PX9.5 |
Synchrotron site | SRS |
Beamline | PX9.5 |
Temperature [K] | 293 |
Detector technology | IMAGE PLATE |
Collection date | 1997-01 |
Detector | MARRESEARCH |
Spacegroup name | P 41 21 2 |
Unit cell lengths | 79.660, 79.660, 463.790 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 10.000 - 3.300 |
R-factor | 0.22 |
Rwork | 0.218 |
R-free | 0.26300 * |
Structure solution method | MOLECULAR REPLACEMENT AND SINGLE ISOMORPHOUS REPLACEMENT |
Starting model (for MR) | 1msp |
RMSD bond length | 0.021 |
RMSD bond angle | 21.900 * |
Data reduction software | MOSFLM |
Data scaling software | CCP4 ((SCALA)) |
Phasing software | AMoRE |
Refinement software | TNT (5D) |
Data quality characteristics
Overall | |
Low resolution limit [Å] | 50.000 |
High resolution limit [Å] | 3.300 |
Rmerge | 0.118 |
Total number of observations | 279016 * |
Number of reflections | 23854 |
<I/σ(I)> | 5.7 |
Completeness [%] | 100.0 |
Redundancy | 11.7 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion * | 7.4 * | 20 * | PROTEIN WAS CRYSTALLIZED FROM 16% PEG 6000, 80MM AMMONIUM SULFATE, 100MM TRIS - HCL, PH 8.5 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 30 (mg/ml) | |
2 | 1 | drop | ammonium sulfate | 40 (mM) | |
3 | 1 | drop | Tris-HCl | 5 (mM) | |
4 | 1 | drop | dithiothreitol | 1 (mM) | |
5 | 1 | reservoir | PEG6000 | 16 (%) | |
6 | 1 | reservoir | ammonium sulfate | 80 (mM) | |
7 | 1 | reservoir | Tris-HCl | 100 (mM) |