Structure determination of tubular crystals of membrane proteins. III. Solvent flattening.
Ultramicroscopy
; 84(1-2): 29-45, 2000 Jul.
Article
em En
| MEDLINE
| ID: mdl-10896138
ABSTRACT
Solvent flattening is considered to be a principal means for improving the data quality in X-ray crystallography. It could be equally effective for tubular crystals of membrane proteins imaged by electron microscopy because of the large empty space inside the tubes. However, tubular crystals are difficult objects for solvent flattening due to lack of electron diffraction amplitudes. Therefore, solvent flattening was used to align images more accurately and to improve the completeness of the data by reducing contributions of noise in the solvent (+ lipid) region. The methods developed were tested with the tubular crystals of Ca2+-ATPase embedded in amorphous ice. The improvement of the data quality was remarkable when solvent flattening was applied to many individual images before averaging. In this way, noises contaminated in the protein region by contrast transfer function were removed effectively. Solvent flattening was far more powerful than simple averaging described in Part II of this series (K. Yonekura, C. Toyoshima, Ultramicroscopy 84 (2000) 15).
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Processamento de Imagem Assistida por Computador
/
Microscopia Eletrônica
/
ATPases Transportadoras de Cálcio
/
Modelos Teóricos
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Ultramicroscopy
Ano de publicação:
2000
Tipo de documento:
Article
País de afiliação:
Japão