1N9K

Crystal structure of the bromide adduct of AphA class B acid phosphatase/phosphotransferase from E. coli at 2.2 A resolution

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X31
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X31
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-05-08
Detector	MARRESEARCH
Wavelength(s)	0.91957, 0.9204, 0.88561
Spacegroup name	P 21 21 2
Unit cell lengths	49.499, 92.616, 138.247
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	25.000 * - 2.200
R-factor	0.19069
Rwork	0.189
R-free	0.23100 *
Structure solution method	MAD
RMSD bond length	0.030 *
RMSD bond angle	1.900 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000 *	2.230
High resolution limit [Å]	2.200	2.200
Rmerge	0.092	0.330
Total number of observations	256647 *
Number of reflections	32501 *	1272 *
<I/σ(I)>	8	3.9
Completeness [%]	98.5 *	96.6
Redundancy	7.3 *	7.0 *

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7.2	293	AphA 6mg/mL, 50 mM Na acetate, 25% PEG 6000 , pH 7.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K The crystals of the native enzyme (containing Mg2+ or Zn2+) have been soaked in 1 M solution of NaBr

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	reservoir	PEG6000	17-22 (%)
3	1	reservoir		1 (mM)