Reduction of lattice disorder in protein crystals by high-pressure cryocooling.
J Appl Crystallogr
; 49(Pt 1): 149-157, 2016 Feb 01.
Article
em En
| MEDLINE
| ID: mdl-26937238
ABSTRACT
High-pressure cryocooling (HPC) has been developed as a technique for reducing the damage that frequently occurs when macromolecular crystals are cryocooled at ambient pressure. Crystals are typically pressurized at around 200â
MPa and then cooled to liquid nitrogen temperature under pressure; this process reduces the need for penetrating cryoprotectants, as well as the damage due to cryocooling, but does not improve the diffraction quality of the as-grown crystals. Here it is reported that HPC using a pressure above 300â
MPa can reduce lattice disorder, in the form of high mosaicity and/or nonmerohedral twinning, in crystals of three different proteins, namely human glutaminase C, the GTP pyrophosphokinase YjbM and the uncharacterized protein lpg1496. Pressure lower than 250â
MPa does not induce this transformation, even with a prolonged pressurization time. These results indicate that HPC at elevated pressures can be a useful tool for improving crystal packing and hence the quality of the diffraction data collected from pressurized crystals.
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1
Coleções:
01-internacional
Base de dados:
MEDLINE
Idioma:
En
Revista:
J Appl Crystallogr
Ano de publicação:
2016
Tipo de documento:
Article
País de afiliação:
Estados Unidos