5EB4

The crystal structure of almond HNL, PaHNL5 V317A, expressed in Aspergillus niger

Experimental procedure

Experimental method	SINGLE WAVELENGTH
Source type	SYNCHROTRON
Source details	SLS BEAMLINE X06SA
Synchrotron site	SLS
Beamline	X06SA
Temperature [K]	100
Detector technology	CCD
Collection date	2011-05-29
Detector	MARMOSAIC 225 mm CCD
Wavelength(s)	1.0
Spacegroup name	P 1 21 1
Unit cell lengths	68.880, 92.300, 97.590
Unit cell angles	90.00, 93.73, 90.00

Refinement procedure

Resolution	49.090 - 2.300
R-factor	0.18954
Rwork	0.186
R-free	0.24704
Structure solution method	MOLECULAR REPLACEMENT
Starting model (for MR)	1ju2
RMSD bond length	0.013
RMSD bond angle	1.708
Data reduction software	XDS
Data scaling software	XDS
Phasing software	PHASER
Refinement software	REFMAC (5.8.0131)

Data quality characteristics

	Overall	Outer shell
Low resolution limit [Å]	49.100	2.350
High resolution limit [Å]	2.300	2.300
Rmerge	0.188	0.566
Number of reflections	49502
<I/σ(I)>	6.6	2.5
Completeness [%]	91.4	85.2
Redundancy	5.3	3.6

Crystallization Conditions

crystal ID	method	pH	temperature	details
1	VAPOR DIFFUSION, SITTING DROP		298	The initial protein concentration was 28 mg/ml (10mM L-Malic acid, MES, Tris pH 7). Different crystal forms were obtained under crystallization conditions varying - PEG 4K, isopropanol and 10mM Hepes pH 7-7.8 with protein concentration 19-28 mg/ml. Most of the crystals that appeared within 2 weeks had visual grow defects. In one of the drops the stack of thin plates appeared after 1 month and one complete dataset was collected.