A brief history of protein crystal growth

McPherson, Alexander

doi:10.1016/0022-0248(91)90859-4

Cited by 78 publications

(51 citation statements)

References 30 publications

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“…The first protein crystals, of hemoglobin from worms and fishes (Hunte et al, 2003;Funke, 1851;Reichert & Brown, 1909;Hunefeld, 1840), were observed more than 150 years ago by German biologists (see McPherson, 1991McPherson, , 1999, for reviews of the history of protein crystal growth). They remained a laboratory curiosity for many years until the 1880s, when Ritthausen (1880Ritthausen ( , 1881 and Osborne (1891Osborne ( , 1892Osborne ( , 1894Osborne ( , 1899 crystallized, for the purpose of purification, a series of plant seed proteins.…”

Section: Some Historymentioning

confidence: 99%

Introduction to protein crystallization

McPherson

Gavira

2013

Acta Crystallogr F Struct Biol Commun

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Protein crystallization was discovered by chance about 150 years ago and was developed in the late 19th century as a powerful purification tool and as a demonstration of chemical purity. The crystallization of proteins, nucleic acids and large biological complexes, such as viruses, depends on the creation of a solution that is supersaturated in the macromolecule but exhibits conditions that do not significantly perturb its natural state. Supersaturation is produced through the addition of mild precipitating agents such as neutral salts or polymers, and by the manipulation of various parameters that include temperature, ionic strength and pH. Also important in the crystallization process are factors that can affect the structural state of the macromolecule, such as metal ions, inhibitors, cofactors or other conventional small molecules. A variety of approaches have been developed that combine the spectrum of factors that effect and promote crystallization, and among the most widely used are vapor diffusion, dialysis, batch and liquid-liquid diffusion. Successes in macromolecular crystallization have multiplied rapidly in recent years owing to the advent of practical, easy-to-use screening kits and the application of laboratory robotics. A brief review will be given here of the most popular methods, some guiding principles and an overview of current technologies.

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Section: Some Historymentioning

confidence: 99%

Introduction to protein crystallization

McPherson

Gavira

2013

Acta Crystallogr F Struct Biol Commun

Self Cite

360

323

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“…The mechanisms underlying this radiation resistance have been studied by several groups, and different hypotheses have been proposed over the years, such as a condensed nucleoid structure, efficient DNA repair pathways, and a higher cellular Mn/Fe ratio [4,[7][8][9][10]. In order to detoxify the reactive oxygen species (ROS) formed under degrading conditions such as exposure to radiation, D. radiodurans possesses an enzymatic antioxidant system comprising superoxide dismutases, peroxidases and catalases that target the primary ROS, the superoxide radical and hydrogen peroxide [11][12][13][14][15][16]. Initial studies on the antioxidant activities of D. radiodurans extracts indicated that this organism contains more than one catalase.…”

Section: Introductionmentioning

confidence: 99%

“…The three amino acids involved in the catalytic center are conserved among catalases: the proximal ligand is a tyrosine that coordinates the heme iron; a histidine and an asparagine located on the opposite, distal side of the heme plane also play a role in the catalytic mechanism. Although catalase was one of the first proteins to be crystallized (in 1937), the first catalase crystal structures only became available 40 years later: the bovine liver [Protein Data Bank (PDB) 1CAT] and the Penicillium vitale (PDB 4CAT) catalases [11][12][13][14].…”

Section: Introductionmentioning

confidence: 99%

Structure of the monofunctional heme catalase DR1998 from Deinococcus radiodurans

et al. 2014

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Deinococcus radiodurans is an aerobic organism with the ability to survive under conditions of high radiation doses or desiccation. As part of its protection system against oxidative stress, this bacterium encodes three monofunctional catalases. The DR1998 catalase belongs to clade 1, and is present at high levels under normal growth conditions. The crystals of DR1998 diffracted very weakly, and the merged diffraction data showed an R sym of 0.308. Its crystal structure was determined and refined to 2.6 Å. The four molecules present in the asymmetric unit form, by crystallographic symmetry, two homotetramers with 222 point‐group symmetry. The overall structure of DR1998 is similar to that of other monofunctional catalases, showing higher structural homology with the catalase structures of clade 1. Each monomer shows the typical catalase fold, and contains one heme b in the active site. The heme is coordinated by the proximal ligand Tyr369, and on the heme distal side the essential His81 and Asn159 are hydrogen‐bonded to a water molecule. A 25‐Å‐long channel is the main channel connecting the active site to the external surface. This channel starts with a hydrophobic region from the catalytic heme site, which is followed by a hydrophilic region that begins on Asp139 and expands up to the protein surface. Apart from this channel, an alternative channel, also near the heme active site, is presented and discussed. Database Coordinates and structure factors have been deposited in the Protein Data Bank in Europe under accession code http://www.rcsb.org/pdb/search/structidSearch.do?structureId=4CAB

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“…The important point is that nucleation is difficult and improbable; growth of preexisting crystals is by contrast easier and more likely. Nucleation is characterized by a distinct series of events, and exactly these events do not need pertain to growth, which is the ordered addition of molecules to a growing lattice (McPherson & Weickmann, 1990;McPherson, 1991).…”

Section: The Nucleation Kineticsmentioning

confidence: 99%