1CJD
THE BACTERIOPHAGE PRD1 COAT PROTEIN, P3, IS STRUCTURALLY SIMILAR TO HUMAN ADENOVIRUS HEXON
Experimental procedure
Experimental method | MAD |
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 100 |
Detector technology | CCD |
Collection date | 1997-06-01 |
Detector | BRANDEIS |
Wavelength(s) | 0.9500, 0.9786, 0.9790 |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 117.956, 121.296, 126.387 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 35.000 - 1.850 |
R-factor | 0.178 * |
Rwork | 0.178 |
R-free | 0.20500 |
Structure solution method | MAD |
RMSD bond length | 0.012 |
RMSD bond angle | 1.800 |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Phasing software | PHASES |
Refinement software | X-PLOR (3.851) |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 35.000 | 1.900 |
High resolution limit [Å] | 1.850 | 1.800 |
Rmerge | 0.046 * | |
Number of reflections | 151224 | |
<I/σ(I)> | 12 | 9 |
Completeness [%] | 99.8 | 91.6 |
Redundancy | 5.2 | 2 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.5 * | 35% (W/V) MPD, 0.2 M NACL, 0.1 M SODIUM ACETATE, PH 4.2 |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | protein | 5 (mg/ml) | |
2 | 1 | drop | Tris-HCl | 10 (mM) | |
3 | 1 | drop | 300 (mM) | ||
4 | 1 | reservoir | MPD | 35 (%(v/v)) | |
5 | 1 | reservoir | sodium acetate | 100 (mM) | |
6 | 1 | reservoir | 200 (mM) |