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 method	MAD
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-1
Synchrotron site	ESRF
Beamline	ID14-1
Temperature [K]	110
Collection date	2000-10-15
Spacegroup name	P 31
Unit cell lengths	67.670, 67.670, 50.200
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	20.000 - 1.800
R-factor	0.182
Rwork	0.182
R-free	0.20400
Structure solution method	MAD
RMSD bond length	0.005
RMSD bond angle	18.900 *
Data reduction software	DENZO
Data scaling software	CCP4
Phasing software	MLPHARE
Refinement software	CNS (0.9)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	1.850
High resolution limit [Å]	1.800	1.800
Rmerge	0.047 *	0.198 *
Total number of observations	95808 *
Number of reflections	23850
<I/σ(I)>	12.4	3.6
Completeness [%]	99.5	99.5
Redundancy	4	4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	4.5	20 *	100 MM NA CITRATE PH 4.5, 17% PEG 2K MME, 10% GLYCEROL

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	5-6 (mg/ml)
2	1	reservoir	PEG2000 MME	17 (%)
3	1	reservoir	sodium citrate	100 (mM)
4	1	reservoir	glycerol	10 (%)
5	1	reservoir	dithiothreitol	10 (mM)