PDBsum entry 1n4f

Hydrolase

PDB id: 1n4f

Contents

Protein chain

129 a.a. *

Ligands

ASR ×3

EDO ×5

Metals

_NA

Waters ×121

* Residue conservation analysis

PDB id:

1n4f

Name:

Hydrolase

Title:

Para-arsanilate derivative of hen egg-white lysozyme

Structure:

LysozymE C. Chain: a. Synonym: 1,4-beta-n-acetylmuramidasE C, allergen gal d 4, gal d iv. Ec: 3.2.1.17

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Other_details: hen egg white

Resolution:

1.78Å R-factor: 0.164 R-free: 0.213

Authors:

P.Retailleau,T.Prange

Key ref:

P.Retailleau and T.Prangé (2003). Phasing power at the K absorption edge of organic arsenic. Acta Crystallogr D Biol Crystallogr, 59, 887-896. PubMed id: 12777806 DOI: 10.1107/S0907444903003512

Date:

31-Oct-02 Release date: 06-May-03

Protein chain

P00698  (LYSC_CHICK) -  Lysozyme C from Gallus gallus

Seq: 147 a.a.

Struc: 129 a.a.

Enzyme reactions

• Enzyme class: E.C.3.2.1.17 - lysozyme.
• Reaction: Hydrolysis of the 1,4-beta-linkages between N-acetyl-D-glucosamine and N-acetylmuramic acid in peptidoglycan heteropolymers of the prokaryotes cell walls.

DOI no: 10.1107/S0907444903003512

Acta Crystallogr D Biol Crystallogr 59:887-896 (2003)

PubMed id: 12777806

Phasing power at the K absorption edge of organic arsenic.

P.Retailleau, T.Prangé.

ABSTRACT

Single/multiple-wavelength anomalous dispersion (SAD/MAD) experiments were performed on a crystal of an organic arsenic derivative of hen egg-white lysozyme. A para-arsanilate compound used as a crystallizing reagent was incorporated into the ordered solvent region of the lysozyme molecule. Diffraction data were collected to high resolution (</=2.0 A) at three wavelengths around the K edge (1.04 A) of arsenic at beamline BM30A, ESRF synchrotron. Anomalous Patterson maps clearly showed the main arsanilate site to be between three symmetry-related lysozyme molecules, at a location previously occupied by a para-toluenesulfonate anion. MAD phases at 2 A derived using the program SHARP led to an electron-density map of sufficient quality to start manual building of the protein model. Amplitudes from a second crystal measured to a resolution of 1.8 A at the peak wavelength revealed two additional heavy-atom sites, which reinforced the anomalous subset model and therefore dramatically improved the phasing power of the arsenic derivative. The subsequent solvent-flattened map was of such high accuracy that the program ARP/wARP was able to build a nearly complete model automatically. This work emphasizes the great potential of arsenic for de novo structure determination using anomalous dispersion methods.

Selected figure(s)

Figure 2.
Figure 2 Resolution-dependent statistics of the anomalous signal and of quality indicators for two different data sets (blue for crystal 1 and black for crystal 2): | F[anom]|/ ( F[anom]) and I/ (I) on the left y axis are absolute numbers, whereas R[sym] and | F[anom]|/F are measured in percentages on the right y axis.

Figure 3.
Figure 3 {w = 1/2, 0 [216]<= u [217]<= 1/2, 0 [218]<= v [219]<= 1/2} Harker sections of anomalous difference Patterson maps for (a) crystal 1 and (b) crystal 2. Levels are contoured in 1 [220][sigma] steps starting at 2 [221][sigma] .

The above figures are reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (2003, 59, 887-896) copyright 2003.

Figures were selected by an automated process.