1AVP
STRUCTURE OF HUMAN ADENOVIRUS 2 PROTEINASE WITH ITS 11 AMINO ACID COFACTOR
Experimental procedure
Source type | SYNCHROTRON |
Source details | NSLS BEAMLINE X12C |
Synchrotron site | NSLS |
Beamline | X12C |
Temperature [K] | 300 |
Detector technology | DIFFRACTOMETER |
Collection date | 1995-05-10 |
Detector | ENRAF-NONIUS FAST |
Spacegroup name | P 61 |
Unit cell lengths | 114.300, 114.300, 50.000 |
Unit cell angles | 90.00, 90.00, 120.00 |
Refinement procedure
Resolution | 6.000 - 2.600 |
R-factor | 0.184 |
Rwork | 0.184 |
R-free | 0.23300 |
Structure solution method | SIRAS SOFTWARE USED : NULL STARTING MODEL FOR MOLECULAR REPLACEMENT: NULL |
RMSD bond length | 0.008 |
RMSD bond angle | 23.600 * |
Data reduction software | DENZO |
Data scaling software | SCALEPACK |
Refinement software | X-PLOR |
Data quality characteristics
Overall | Outer shell | |
Low resolution limit [Å] | 50.000 | 2.690 |
High resolution limit [Å] | 2.600 | 2.600 |
Rmerge | 0.077 | 0.145 |
Number of reflections | 11559 | |
<I/σ(I)> | 20 | 16 |
Completeness [%] | 98.8 | 97.6 |
Redundancy | 5 | 6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 7.5 * | McGrath, W.J., (1996) J. Struct. Biol., 117, 77. * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | reservoir | HEPES | 100 (mM) | pH7.5 |
2 | 1 | reservoir | sodium acetate | 1.4-1.6 (M) |