1HYN

CRYSTAL STRUCTURE OF THE CYTOPLASMIC DOMAIN OF HUMAN ERYTHROCYTE BAND-3 PROTEIN

Experimental procedure

Experimental method	MAD
Source type	SYNCHROTRON
Source details	APS BEAMLINE 14-BM-D
Synchrotron site	APS
Beamline	14-BM-D
Temperature [K]	108
Detector technology	CCD
Collection date	1998-09-23
Detector	ADSC QUANTUM 1
Wavelength(s)	0.9789, 0.9796, 0.9537
Spacegroup name	C 1 2 1
Unit cell lengths	181.590, 92.580, 123.330
Unit cell angles	90.00, 131.86, 90.00

Refinement procedure

Resolution	8.000 - 2.600
R-factor	0.216 *
Rwork	0.216
R-free	0.29000
Structure solution method	MAD
RMSD bond length	0.008 *
RMSD bond angle	1.210 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	SOLVE
Refinement software	X-PLOR

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	35.000 *	2.680
High resolution limit [Å]	2.590	2.590
Rmerge	0.057 *	0.208 *
Number of reflections	46609
<I/σ(I)>	37.16	18.7
Completeness [%]	99.1 *	94.5 *
Redundancy	3.8	2.8

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7.4 *		Kiyatkin, A., (1995) Proteins: Struct., Funct., Genet., 22, 293. *

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	1.2-2 (mg/ml)
10	1	reservoir	sodium azide	1 (mM)
2	1	drop	sodium phosphate	5 (mM)
3	1	drop		150 (mM)
4	1	drop	EDTA	1 (mM)
5	1	drop	sodium azide	1 (mM)
6	1	drop	dithiothreitol	1 (mM)
7	1	drop	glycerol	30 (%(v/v))
8	1	reservoir	ammonium sulfate	65-68 (%sat)
9	1	reservoir	sodium citrate	150 (mM)