1PHK
TWO STRUCTURES OF THE CATALYTIC DOMAIN OF PHOSPHORYLASE, KINASE: AN ACTIVE PROTEIN KINASE COMPLEXED WITH NUCLEOTIDE, SUBSTRATE-ANALOGUE AND PRODUCT
Experimental procedure
Source type | SYNCHROTRON |
Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
Synchrotron site | EMBL/DESY, HAMBURG |
Beamline | BW7B |
Detector technology | CCD |
Collection date | 1994-11-05 |
Detector | MARRESEARCH |
Spacegroup name | P 21 21 21 |
Unit cell lengths | 47.600, 67.400, 110.800 |
Unit cell angles | 90.00, 90.00, 90.00 |
Refinement procedure
Resolution | 6.000 - 2.200 |
R-factor | 0.21 |
Rwork | 0.210 |
R-free | 0.28800 |
RMSD bond length | 0.010 |
Data reduction software | DENZO |
Phasing software | X-PLOR |
Refinement software | X-PLOR |
Data quality characteristics
Overall | |
High resolution limit [Å] | 2.100 |
Rmerge | 0.074 |
Number of reflections | 19961 |
Completeness [%] | 88.8 |
Redundancy | 3.6 |
Crystallization Conditions
crystal ID | method | pH | temperature | details |
1 | Vapor diffusion, hanging drop * | 8.2 * | 14 * |
Crystallization Reagents in Literatures
ID | crystal ID | solution | reagent name | concentration (unit) | details |
1 | 1 | drop | Phk gamma trnc | 10-12 (mg/ml) | |
10 | 1 | reservoir | 10 (mM) | ||
11 | 1 | reservoir | glycerol | 10 (%(v/v)) | |
12 | 1 | reservoir | DTT | 10 (mM) | |
13 | 1 | reservoir | 0.02 (%(w/v)) | ||
2 | 1 | drop | AMPPNP | 3 (mM) | |
3 | 1 | drop | HEPES/NaOH | 10 (mM) | |
4 | 1 | drop | glycerol | 2 (%(v/v)) | |
5 | 1 | drop | DTT | 10 (mM) | |
6 | 1 | drop | 0.02 (%(w/v)) | ||
7 | 1 | drop | EDTA | 0.1 (mM) | |
8 | 1 | reservoir | PEG8000 | 5 (%(w/v)) | |
9 | 1 | reservoir | HEPES/NaOH | 50 (mM) |