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1HH8

The active N-terminal region of p67phox: Structure at 1.8 Angstrom resolution and biochemical characterizations of the A128V mutant implicated in chronic granulomatous disease

Experimental procedure
Experimental methodMAD
Source typeSYNCHROTRON
Source detailsESRF BEAMLINE ID14-1
Synchrotron siteESRF
BeamlineID14-1
Temperature [K]110
Collection date2000-10-15
Spacegroup nameP 31
Unit cell lengths67.670, 67.670, 50.200
Unit cell angles90.00, 90.00, 120.00
Refinement procedure
Resolution20.000 - 1.800
R-factor0.182
Rwork0.182
R-free0.20400
Structure solution methodMAD
RMSD bond length0.005
RMSD bond angle18.900

*

Data reduction softwareDENZO
Data scaling softwareCCP4
Phasing softwareMLPHARE
Refinement softwareCNS (0.9)
Data quality characteristics
 OverallOuter shell
Low resolution limit [Å]20.0001.850
High resolution limit [Å]1.8001.800
Rmerge0.047

*

0.198

*

Total number of observations95808

*

Number of reflections23850
<I/σ(I)>12.43.6
Completeness [%]99.599.5
Redundancy44
Crystallization Conditions
crystal IDmethodpHtemperaturedetails
1Vapor diffusion, hanging drop

*

4.520

*

100 MM NA CITRATE PH 4.5, 17% PEG 2K MME, 10% GLYCEROL
Crystallization Reagents in Literatures
IDcrystal IDsolutionreagent nameconcentration (unit)details
11dropprotein5-6 (mg/ml)
21reservoirPEG2000 MME17 (%)
31reservoirsodium citrate100 (mM)
41reservoirglycerol10 (%)
51reservoirdithiothreitol10 (mM)

224201

PDB entries from 2024-08-28

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