1E6O

Crystal structure of Fab13B5 against HIV-1 capsid protein p24

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	ESRF BEAMLINE BM14
Synchrotron site	ESRF
Beamline	BM14
Temperature [K]	100
Detector technology	IMAGE PLATE
Collection date	1997-04-15
Detector	MARRESEARCH
Spacegroup name	P 21 21 21
Unit cell lengths	36.680, 81.900, 134.400
Unit cell angles	90.00, 90.00, 90.00

Refinement procedure

Resolution	15.000 - 1.800
R-factor	0.225
Rwork	0.225
R-free	0.25500
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1afv
RMSD bond length	0.005
RMSD bond angle	1.400
Data reduction software	MOSFLM
Data scaling software	SCALA
Phasing software	X-PLOR (3.8)
Refinement software	X-PLOR (3.8)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	15.000	1.850
High resolution limit [Å]	1.800	1.800
Rmerge	0.063 *	0.128 *
Total number of observations	124392 *
Number of reflections	35964
Completeness [%]	94.0	85.5 *
Redundancy	3.5	3.5

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	7.8	22 *	7MG/ML OF FAB'13B5 IN 0.1M PIPES PH=7.8 IN 9% TO 11% PEG8000 AFTER EQUILIBRATION IN HANGING DROPS AT 22C, pH 7.80

Crystallization Reagents in Literatures

ID	crystal ID	solution	reagent name	concentration (unit)	details
1	1	reservoir	PEG8000	9-11 (%)
2	1	reservoir	PIPES	0.1 (M)