3ZZI

Crystal structure of a tetrameric acetylglutamate kinase from Saccharomyces cerevisiae

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE ID14-4
Synchrotron site	ESRF
Beamline	ID14-4
Temperature [K]	100
Detector technology	CCD
Collection date	2011-03-03
Detector	ADSC CCD
Spacegroup name	P 1
Unit cell lengths	95.240, 111.290, 113.140
Unit cell angles	75.77, 89.29, 69.12

Refinement procedure

Resolution	109.110 - 3.800
R-factor	0.19914
Rwork	0.197
R-free	0.23592
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	3ZZF FOR ONE DOMAIN AND AN INCOMPLETE TRACING FROM OTHER CRYSTAL OF THE SAME PRESENT PROTEIN FOR THE SECOND DOMAIN
RMSD bond length	0.015
RMSD bond angle	1.793
Data reduction software	XDS
Data scaling software	SCALA
Phasing software	MOLREP
Refinement software	REFMAC (5.6.0117)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	109.000	4.010
High resolution limit [Å]	3.800	3.800
Rmerge	0.057	0.455
Number of reflections	39773
<I/σ(I)>	10.5	1.5
Completeness [%]	96.3	96.3
Redundancy	2.4	2.4

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP	7	277	PROTEIN WAS SUBJECTED TO REDUCTIVE METHYLATION OF SURFACE EXPOSED LYSINES WITH ABC PREVIOUS TO CRYSTALLIZATION. 10 MG/ML PROTEIN IN 20MM HEPES PH 7.5, 0.5 M NACL, 1MM MSH, AND SUPPLEMENTED WITH 40 MM NAG, WAS CRYSTALLIZED IN PRESENCE OF 0.2 M AMMONIUM CITRATE PH 7.0 AND 12 % PEG3350 AS CRYSTALLIZATION SOLUTION, IN SITTING DROPS AT 4C. CRYOBUFFER SOLUTION WAS THAT OF CRYSTALLIZATION WITH PEG3350 ENRICHED TO 40 %.