1I5O

CRYSTAL STRUCTURE OF MUTANT R105A OF E. COLI ASPARTATE TRANSCARBAMOYLASE

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	ROTATING ANODE
Source details	RIGAKU RU200
Temperature [K]	295
Detector technology	AREA DETECTOR
Collection date	1996-07-25
Detector	UCSD MARK II
Wavelength(s)	1.5418
Spacegroup name	P 3 2 1
Unit cell lengths	122.250, 122.250, 142.670
Unit cell angles	90.00, 90.00, 120.00

Refinement procedure

Resolution	10.000 - 2.800
R-factor	0.155 *
Rwork	0.155
R-free	0.21200
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	5at1
RMSD bond length	0.017
RMSD bond angle	24.300 *
Data reduction software	SDMS
Data scaling software	SDMS
Phasing software	X-PLOR
Refinement software	X-PLOR (3.1)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	2.990
High resolution limit [Å]	2.780	2.780
Rmerge	0.099	0.370
Total number of observations	90537 *
Number of reflections	29390
<I/σ(I)>	5.75	1
Completeness [%]	93.0	75
Redundancy	3.08	1.85

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	MICRODIALYSIS	5.75 *	20 *	Jin, L., (2000) Biochemistry, 39, 8058. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	1	enzyme	7.5 (mg/ml)
2	1	2	PALA	1 (mM)
3	1	2	maleic acid	20 (mM)
4	1	2	sodium azide	3 (mM)