1AK4

HUMAN CYCLOPHILIN A BOUND TO THE AMINO-TERMINAL DOMAIN OF HIV-1 CAPSID

Experimental procedure

Source type	SYNCHROTRON
Source details	NSLS BEAMLINE X12B
Synchrotron site	NSLS
Beamline	X12B
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1996-06
Detector	MARRESEARCH
Spacegroup name	P 1 21 1
Unit cell lengths	38.600, 113.100, 67.000
Unit cell angles	90.00, 100.70, 90.00

Refinement procedure

Resolution	6.000 - 2.360
R-factor	0.238
Rwork	0.238
R-free	0.30600
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	CYPA STRUCTURE (PDB ENTRY 2CYH)
RMSD bond length	0.005
RMSD bond angle	1.300
Data reduction software	DENZO
Data scaling software	SCALEPACK
Phasing software	X-PLOR (3.843)
Refinement software	X-PLOR (3.843)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	20.000	2.400
High resolution limit [Å]	2.360	2.360
Rmerge	0.110 *	0.399 *
Number of reflections	21503	1049 *
<I/σ(I)>	10.5	3.5
Completeness [%]	97.0	91

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	Vapor diffusion, sitting drop *	7	21 *	THE PROTEIN SOLUTION WAS 0.25 MM CYPA AND 0.25 MM CA(151) IN 10 MM TRISHCL (PH 8.0) AND 1 MM 2-MERCAPTOETHANOL. THE RESERVOIR SOLUTION WAS 1ML OF 1.0 M LICL, 0.1 M BICINE (PH 7.0), AND 22% POLYETHYLENE GLYCOL 8000. THE INITIAL DROP WAS 6 MICROL OF A 1:1 MIX OF PROTEIN AND RESERVOIR SOLUTIONS.

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	drop	CyPA	0.125 (mM)
10	1	reservoir	PEG8000	22 (%)
2	1	drop	CA151	0.125 (mM)
3	1	drop	Tris-HCl	5 (mM)
4	1	drop	2-mercaptoethanol	0.5 (mM)
5	1	drop		0.50 (M)
6	1	drop	Bicine	0.50 (M)
7	1	drop	PEG8000	11 (%)
8	1	reservoir		1.0 (M)
9	1	reservoir	Bicine	0.1 (M)