An improved method for protein crystal density measurements

1999 ◽  
Vol 32 (5) ◽  
pp. 1006-1009 ◽  
Author(s):  
Adelaine K. W. Leung ◽  
Michael M. V. Park ◽  
David W. Borhani
Keyword(s):  
Protein Crystal ◽  
Protein Crystals ◽  
Density Gradients ◽  
Hen Egg White Lysozyme ◽  
Human Apolipoprotein ◽  
Egg White Lysozyme ◽  
Crystal Density ◽  
Solvent Density ◽  
Hen Egg White

Determination of the density of protein crystals by flotation in organic solvent density gradients using simple methods for the preparation of the density gradients and the transfer of crystals into these gradients is described. The method was tested with crystals of hen egg white lysozyme. These methods are especially suitable for use with fragile, high-solvent-content protein crystals. These methods were applied to the measurement of the density of human apolipoprotein A-I crystals.

scholarly journals Structure Determination of Hen Egg-White Lysozyme Aggregates Adsorbed to Lipid/Water and Air/Water Interfaces

Langmuir ◽  
2020 ◽  
Vol 36 (17) ◽  
pp. 4766-4775
Author(s):  
S. Strazdaite ◽  
E. Navakauskas ◽  
J. Kirschner ◽  
T. Sneideris ◽  
G. Niaura
Keyword(s):  
Structure Determination ◽  
Egg White ◽  
Hen Egg White Lysozyme ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Hen Egg

Digital topography with an X-ray CCD camera for characterizing perfection in protein crystals

2012 ◽  
Vol 45 (5) ◽  
pp. 1009-1014 ◽  
Author(s):  
Kei Wako ◽  
Kunio Kimura ◽  
Yu Yamamoto ◽  
Takuya Sawaura ◽  
Mengyuan Shen ◽  
...  
Keyword(s):  
Ccd Camera ◽  
Egg White ◽  
Protein Crystals ◽  
Hen Egg White Lysozyme ◽  
X Ray ◽  
Crystal Perfection ◽  
Egg White Lysozyme ◽  
Domain Structures ◽  
Peak Broadening ◽  
Hen Egg White

Digital X-ray topography using an X-ray CCD camera and conventional X-ray topography using X-ray film were used to investigate tetragonal hen egg-white lysozyme (HEWL) crystals. Previously, clear dislocation images of protein crystals were mainly obtained by film methods. Earlier studies of HEWL crystals using an X-ray CCD camera mainly revealed domain structures. In the present study, dislocation images of the same HEWL crystal have been obtained by using conventional X-ray film and a digital X-ray CCD camera. The results demonstrate that digital topography using an X-ray CCD camera is an effective method for characterizing protein crystals. A series of digital topographic images were analyzed by the method developed by Lovelace, Murphy, Pahl, Brister & Borgstahl [J. Appl. Cryst.(2006),39, 425–432]. Sub-peaks and peak broadening originating from dislocations in local rocking curves were observed. Moreover, the crystal perfection was evaluated by mapping the angular positions of the maximums and the full widths at half-maximum of local rocking curves.

scholarly journals Characterization of dislocations in protein crystals by means of synchrotron double-crystal topography

2004 ◽  
Vol 37 (1) ◽  
pp. 67-71 ◽  
Author(s):  
B. Capelle ◽  
Y. Epelboin ◽  
J. Härtwig ◽  
A. B. Moraleda ◽  
F. Otálora ◽  
...  
Keyword(s):  
Spiral Growth ◽  
Protein Crystals ◽  
Hen Egg White Lysozyme ◽  
Growth Sector ◽  
Double Crystal ◽  
Egg White Lysozyme ◽  
Weak Beam ◽  
Hen Egg White ◽  
Edge Dislocations

Hen egg-white lysozyme (HEWL) crystals have been studied by means of double-crystal synchrotron topography. The crystals reveal a number of features that are quite well known in hydrothermally grown inorganic crystals: dislocations, growth bands and growth sector boundaries. Dislocations in the 〈110〉 sectors have been characterized as edge dislocations with Burgers vector parallel to thecaxis. They are distinguishable only under weak beam conditions. The presence of edge dislocations shown in this paper is consistent with the spiral growth steps previously reported. This spiral growth on protein crystals has been observed many times by surface techniques.

Neutron diffraction studies of proteins

1980 ◽  
Vol 290 (1043) ◽  
pp. 505-510 ◽  
Keyword(s):  
Neutron Diffraction ◽  
Protein Crystallography ◽  
Protein Crystals ◽  
X Rays ◽  
Hen Egg White Lysozyme ◽  
X Ray ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Neutron Protein Crystallography ◽  
Triclinic Form

Neutrons interact differently with protein crystals than do X-rays. Not only do hydrogen or deuterium atoms diffract neutrons relatively more strongly, but in addition protein crystals suffer no radiation damage in a neutron beam. These and other differences are being exploited for a few selected proteins, at three reactors. At the Institut Laue-Langevin, Grenoble, the crystal structure of the triclinic form of hen egg-white lysozyme is being refined at high resolution ( d -spacings down to 1.4 Å (0.14 nm)), from neutron diffraction measurements on a partly deuterated native crystal of volume 20 mm 3 . Results at the present stage of refinement are discussed. Prospects for neutron protein crystallography are examined in the light of progress in X-ray protein crystallography and neutron detector technology.

Analysis of slip systems in protein crystals with triclinic form using the phenomenological macro-bond method

CrystEngComm ◽  
2021 ◽  
Author(s):  
Ryo Suzuki ◽  
Chika Shigemoto ◽  
Marina Abe ◽  
Kenichi Kojima ◽  
Masaru Tachibana
Keyword(s):  
Egg White ◽  
Protein Crystals ◽  
Slip Systems ◽  
Hen Egg White Lysozyme ◽  
Indentation Method ◽  
Egg White Lysozyme ◽  
Hen Egg White ◽  
Triclinic Form ◽  
Hen Egg ◽  
Bond Method

Slip systems in triclinic hen egg-white lysozyme (Tri-HEWL) crystals, which is one of typical protein crystals, were identified by the indentation method. Eleven kinds of the slip systems are clearly...

scholarly journals Protein Crystallography: Getting in on the Ground Floor

2014 ◽  
Vol 70 (a1) ◽  
pp. C931-C931
Author(s):  
Brian Matthews
Keyword(s):  
Three Dimensional ◽  
Protein Crystal ◽  
Dimensional Structure ◽  
Three Dimensional Structure ◽  
Egg White Lysozyme ◽  
Isomorphous Replacement ◽  
Hen Egg White ◽  
Diffraction Patterns ◽  
Dorothy Crowfoot Hodgkin

The first diffraction pattern from crystals of a protein was obtained by Desmond Bernal and Dorothy Crowfoot Hodgkin in 1934. As early as 1939, Bernal described how such diffraction patterns might be used to determine the complete three-dimensional structure of a protein. It was not until 1954, however, that Max Perutz showed how isomorphous replacement could be used to determine the phases for crystalline hemoglobin. Using this approach, Kendrew and coworkers described the three-dimensional structure of myoglobin in 1960. In 1965, David Phillips' group determined the structure of hen egg-white lysozyme. Then, in 1967, three different protein crystal structures were reported. Macromolecular crystallography had come of age. The talk will touch on some of these early events and include reminiscences of work at the MRC Lab in David Blow's group leading up to the successful determination of the alpha-chymotrypsin structure.

scholarly journals Combining random microseed matrix screening and the magic triangle for the efficient structure solution of a potential lysin from bacteriophage P68

2019 ◽  
Vol 75 (7) ◽  
pp. 670-681
Author(s):  
Jia Quyen Truong ◽  
Santosh Panjikar ◽  
Linda Shearwin-Whyatt ◽  
John B. Bruning ◽  
Keith E. Shearwin
Keyword(s):  
Hen Egg White Lysozyme ◽  
High Quality ◽  
X Ray Crystallography ◽  
Egg White Lysozyme ◽  
Structure Solution ◽  
Experimental Phasing ◽  
Sad Phasing ◽  
Hen Egg White ◽  
Novel Structures

Two commonly encountered bottlenecks in the structure determination of a protein by X-ray crystallography are screening for conditions that give high-quality crystals and, in the case of novel structures, finding derivatization conditions for experimental phasing. In this study, the phasing molecule 5-amino-2,4,6-triiodoisophthalic acid (I3C) was added to a random microseed matrix screen to generate high-quality crystals derivatized with I3C in a single optimization experiment. I3C, often referred to as the magic triangle, contains an aromatic ring scaffold with three bound I atoms. This approach was applied to efficiently phase the structures of hen egg-white lysozyme and the N-terminal domain of the Orf11 protein from Staphylococcus phage P68 (Orf11 NTD) using SAD phasing. The structure of Orf11 NTD suggests that it may play a role as a virion-associated lysin or endolysin.

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