1P8F

A four location model to explain the stereospecificity of proteins.

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ALS BEAMLINE 5.0.2
Synchrotron site	ALS
Beamline	5.0.2
Temperature [K]	100
Detector technology	CCD
Collection date	1999-02-05
Detector	ADSC QUANTUM 4
Wavelength(s)	1.00
Spacegroup name	P 43 21 2
Unit cell lengths	103.306, 103.306, 150.004
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	24.860 - 1.850
R-factor	0.192
Rwork	0.192
R-free	0.22500
Structure solution method	MOLECULAR REPLACEMENT
RMSD bond length	0.014
RMSD bond angle	25.100 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR
Refinement software	CNS (1.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	25.000	1.920
High resolution limit [Å]	1.850	1.850
Rmerge	0.073	0.473
Number of reflections	69674
<I/σ(I)>	20.7	3.2
Completeness [%]		98.6
Redundancy	14

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	unknown *	7.5	295	IDH, stored in metal-free final buffer, was diluted to 25, 30, 35 and 40 mg/ml using metal-free 2X buffer; (70mM Na2HPO4 , 18 mM citric acid, 200 mM NaCl, 0.4 mM DTT, pH 5.4). and was crystallized from hanging drops using 5 l each of these IDH solutions and 5 l each of 34, 36, 38, 40, 42, and 44 % (NH4)2SO4 solutions in crystallization buffer (35mM Na2HPO4 , 9 mM citric acid, 100 mM NaCl, 0.2 mM DTT at pH 6.1, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 22K