1IAT

CRYSTAL STRUCTURE OF HUMAN PHOSPHOGLUCOSE ISOMERASE/NEUROLEUKIN/AUTOCRINE MOTILITY FACTOR/MATURATION FACTOR

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SRS BEAMLINE PX7.2
Synchrotron site	SRS
Beamline	PX7.2
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	2000-03-17
Detector	MARRESEARCH
Wavelength(s)	1.488
Spacegroup name	P 43 21 2
Unit cell lengths	94.183, 94.183, 136.138
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	29.880 - 1.620
R-factor	0.1466
Rwork	0.144
R-free	0.17000
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	PIG MUSCLE PGI (unpublished)
RMSD bond length	0.016 *
RMSD bond angle	1.590 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	AMoRE
Refinement software	REFMAC (5.0)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	30.000	1.690
High resolution limit [Å]	1.620	1.620
Rmerge	0.048	0.173
Number of reflections	75504
<I/σ(I)>	30.65	7.33
Completeness [%]	96.4	88.4
Redundancy	5.13	4.52

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.5 *	291	Ammonium sulphate, tris-HCl, Na Hepes, beta-mercaptoethanol, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	ammonium sulfate	2.6 (M)
2	1	reservoir	Tris	100 (mM)
3	1	drop	HEPES	15 (mM)
4	1	drop	beta-mercaptoethanol	2 (mM)
5	1	drop	protein	4 (mg/ml)