2FZC

The Structure of Wild-Type E. Coli Aspartate Transcarbamoylase in Complex with Novel T State Inhibitors at 2.10 Resolution

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	110
Detector technology	IMAGE PLATE
Collection date	2005-01-01
Detector	RIGAKU RAXIS IV
Wavelength(s)	1.5418
Spacegroup name	P 3 2 1
Unit cell lengths	120.590, 120.590, 141.710
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	27.350 - 2.100
R-factor	0.196
Rwork	0.196
R-free	0.25010
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1za1
Data reduction software	d*TREK
Data scaling software	d*TREK
Phasing software	AMoRE
Refinement software	CNS (1.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	27.350	2.070
High resolution limit [Å]	2.000	2.000
Rmerge	0.058	0.362
Number of reflections	80677
<I/σ(I)>	13.5	4.3
Completeness [%]	99.9	99.5
Redundancy	5.31	5.13

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	5.7	298	ATCase holoenzyme was crystallized by microdialysis, using 50 L wells. The enzyme solution, at ~18 mg/mL, was dialyzed against a solution of 40 mM citric acid, 3 mM sodium azide, 1 mM 2-mercaptoethanol, 1 mM cytidine 5 -triphosphate, 0.2 mM EDTA (pH 5.7) , VAPOR DIFFUSION, HANGING DROP, temperature 298K