1IAM

STRUCTURE OF THE TWO AMINO-TERMINAL DOMAINS OF HUMAN INTERCELLULAR ADHESION MOLECULE-1, ICAM-1

Experimental procedure

Source type	SYNCHROTRON
Source details	CHESS BEAMLINE A1
Synchrotron site	CHESS
Beamline	A1
Temperature [K]	120
Detector technology	CCD
Collection date	1995-02-26
Spacegroup name	C 2 2 21
Unit cell lengths	41.857, 124.736, 83.186
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	5.000 - 2.100
R-factor	0.214
Rwork	0.214
R-free	0.30300
Structure solution method	MOLECULAR REPLACEMENT, MIR, PHASE RECOMBINATION
Starting model (for MR)	ICAM-2 PDB ENTRY 1ZXQ
RMSD bond length	0.009
RMSD bond angle	28.200 *
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.851)
Refinement software	X-PLOR (3.851)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.170
High resolution limit [Å]	2.100	2.100
Rmerge	0.036	0.059
Number of reflections	10629
<I/σ(I)>	24.15	10.21
Completeness [%]	81.1	33.4
Redundancy	3	0.3

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, hanging drop *	7.5		PROTEIN IN 10 MM TRIS, PH 7.5, 25 MM NACL, WAS CRYSTALLIZED FROM 20% PEG 4000 IN 10 MM TRIS AS PRECIPITANT

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	protein	10 (mg/ml)
2	1	drop	Tris	10 (mM)
3	1	drop		25 (mM)
4	1	reservoir	PEG4000	20 (%)
5	1	reservoir	Tris	10 (mM)