3SQF

Crystal structure of monomeric M-PMV retroviral protease

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	EMBL/DESY, HAMBURG BEAMLINE X13
Synchrotron site	EMBL/DESY, HAMBURG
Beamline	X13
Temperature [K]	100
Detector technology	CCD
Collection date	2007-12-13
Detector	MAR CCD 165 mm
Wavelength(s)	0.8086
Spacegroup name	P 1 21 1
Unit cell lengths	26.760, 86.620, 39.310
Unit cell angles	90.00, 104.60, 90.00

Refinement procedure

Resolution	28.600 - 1.632
R-factor	0.1715
Rwork	0.169
R-free	0.21240
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	A model generated by Foldit players from the NMR coordinates 1NSO
RMSD bond length	0.019
RMSD bond angle	1.770
Data reduction software	XDS
Data scaling software	XSCALE
Phasing software	PHASER
Refinement software	PHENIX (1.7_641)

Data quality characteristics

	Overall	Inner shell	Outer shell
Low resolution limit [Å]	43.300	43.300	1.730
High resolution limit [Å]	1.630	4.870	1.630
Rmerge	0.068	0.024	0.752
Number of reflections	21369	824	3337
<I/σ(I)>	14.86	44.95	1.9
Completeness [%]	99.0	98.3	96.3
Redundancy	4.7		4.2

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, HANGING DROP	6.5	292	0.1 M imidazole, 1 M sodium acetate, 1.2-fold molar excess (relative to dimeric protein) of Pro-Tyr-Val-Pst-Ala-Met-Thr (inhibitor), pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 292K