1W6C

AGAO holoenzyme in a small cell, at 2.2 angstroms

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SSRL BEAMLINE BL7-1
Synchrotron site	SSRL
Beamline	BL7-1
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2002-03-20
Detector	MAR scanner 345 mm plate
Spacegroup name	C 1 2 1
Unit cell lengths	158.041, 64.061, 69.693
Unit cell angles	90.00, 111.74, 90.00

Refinement procedure

Resolution	32.160 - 2.200
R-factor	0.175
Rwork	0.172
R-free	0.21900
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PDB ENRTY 1AV4
RMSD bond length	0.013
RMSD bond angle	1.451
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	MOLREP
Refinement software	REFMAC (5.1.24)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	28.250	2.270
High resolution limit [Å]	2.200	2.200
Rmerge	0.050	0.290
Number of reflections	31420
<I/σ(I)>	13.68	3.35
Completeness [%]	94.4	84.9
Redundancy	2.2	1.96

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	293	CRYSTALS WERE GROWN IN ABOUT 2 WEEKS BY HANGING-DROP VAPOR DIFFUSION AT 293K. THE RESERVOIR WAS 0.2M MG ACETATE, 20% PEG 8K, 0.1M NA CACODYLATE PH 6.5. THE DROPS WERE 1.5MICROL OF 11.7 MG/ML PROTEIN, 0.05M HEPES, PH 7.0, PLUS 1.5MICROL OF RESERVOIR SOLUTION. A CRYSTAL WAS CRYOPROTECTED BY GRADUAL INCREMENTAL SOAKING IN RESERVOIR SOLUTION MIXED WITH GLYCEROL. THE CONCENTRATION OF GLYCEROL WAS INCREASED FROM 0 TO 30% IN 2-3% INCREMENTS DURING 2 HOURS. THE CRYSTAL WAS THEN FROZEN IN THE CRYOSTREAM.