PDBsum entry: 1bwh

Hydrolase

PDB id: 1bwh

Contents

Protein chain

129 a.a. *

Waters ×92

* Residue conservation analysis

PDB id:

1bwh

Name:

Hydrolase

Title:

The 1.8 a structure of ground control grown tetragonal hen egg white lysozyme

Structure:

Protein (lysozyme). Chain: a. Synonym: gal d iv, allergen gal d 4. Ec: 3.2.1.17

Source:

Gallus gallus. Chicken. Organism_taxid: 9031. Cellular_location: egg white. Other_details: sigma

Resolution:

1.80Å R-factor: 0.184 R-free: 0.233

Authors:

J.Dong,T.J.Boggon,N.E.Chayen,J.Raftery,R.C.Bi

Key ref:

J.Dong et al. (1999). Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 A resolution. Acta Crystallogr D Biol Crystallogr, 55, 745-752. PubMed id: 10089304 DOI: 10.1107/S0907444998016047

Date:

24-Sep-98 Release date: 30-Sep-98

Protein chain

P00698  (LYSC_CHICK) -  Lysozyme C

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.

 Gene Ontology (GO) functional annotation 

• Cellular component: extracellular region (2 terms)
• Biological process: metabolic process (4 terms)
• Biochemical function: catalytic activity (5 terms)

DOI no: 10.1107/S0907444998016047

Acta Crystallogr D Biol Crystallogr 55:745-752 (1999)

PubMed id: 10089304

Bound-solvent structures for microgravity-, ground control-, gel- and microbatch-grown hen egg-white lysozyme crystals at 1.8 A resolution.

J.Dong, T.J.Boggon, N.E.Chayen, J.Raftery, R.C.Bi, J.R.Helliwell.

ABSTRACT

A number of methods can be used to improve the stability of the protein crystal-growth environment, including growth in microgravity without an air-liquid phase boundary, growth in gels and growth under oil ('microbatch'). In this study, X-ray data has been collected from and structures refined for crystals of hen egg-white lysozyme (HEWL) grown using four different methods, liquid-liquid dialysis on Earth and in microgravity using the European Space Agency's (ESA) Advanced Protein Crystallization Facility (APCF) on board the NASA Space Shuttle Life and Microgravity Spacelab (LMS) mission (STS-78), crystallization in agarose gel using a tube liquid-gel diffusion method and crystallization in microbatch under oil. A comparison of the overall quality of the X-ray data, the protein structures and especially the bound-water structures has been carried out at 1.8 A. The lysozyme protein structures corresponding to these four different crystallization methods remain similar. A small improvement in the bound-solvent structure is seen in lysozyme crystals grown in microgravity by liquid-liquid dialysis, which has a more stable fluid physics state in microgravity, and is consistent with a better formed protein crystal in microgravity.

Selected figure(s)

Figure 1.
Figure 1 Average values of /< > plotted against 4sin^2 / ^2 for the microgravity-, ground-control-, gel- and microbatch-grown crystals.

The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 745-752) copyright 1999.

Figure was selected by an automated process.